Localization of Phosphatidylserine Binding Sites to Structural Domains of Factor Xa
Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor Xa by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B. R. (1996) Biochemistry 35, 7482–7491). In the present study, we locate three C6PS binding sites to different domains of factor Xa using a com...
Saved in:
Published in | The Journal of biological chemistry Vol. 277; no. 3; pp. 1855 - 1863 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
18.01.2002
American Society for Biochemistry and Molecular Biology |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor Xa by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B. R. (1996) Biochemistry 35, 7482–7491). In the present study, we locate three C6PS binding sites to different domains of factor Xa using a combination of activity, circular dichroism, fluorescence, and equilibrium dialysis measurements on proteolytic and biosynthetic fragments of factor Xa. Our results demonstrate that the structural responses of human and bovine factor Xa to C6PS binding are somewhat different. Despite this difference, data obtained with fragments from both human and bovine factor Xa are consistent with a common hypothesis for the location of C6PS binding sites to different structural domains. First, the γ-carboxyglutamic acid (Gla) domain binds C6PS only in the absence of Ca2+ (kd ∼ 1 mm), although this PS site does not influence the functional response of factor Xa. Second, a Ca2+-dependent binding site is in the epidermal growth factor domains (EGFNC) that are linked by Ca2+ and C6PS binding to the Gla domain. This site appears to be the lipid regulatory site of factor Xa. Third, a Ca2+-requiring site seems to be in the EGFC-catalytic domain. This site appears not to be a lipid regulatory site but rather to share residues with the substrate recognition site. Finally, the full functional response to C6PS requires linkage of the Gla, EGFNC, and catalytic domains in the presence of Ca2+, meaning that PS regulation of factor Xa involves linkage between widely separated parts of the protein. |
---|---|
AbstractList | Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor X a by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B. R. (1996) Biochemistry 35, 7482â7491). In the present study, we locate three C6PS binding sites to different domains of factor X a using a combination of activity, circular dichroism, fluorescence, and equilibrium dialysis measurements on proteolytic and
biosynthetic fragments of factor X a . Our results demonstrate that the structural responses of human and bovine factor X a to C6PS binding are somewhat different. Despite this difference, data obtained with fragments from both human and bovine
factor X a are consistent with a common hypothesis for the location of C6PS binding sites to different structural domains. First, the
γ-carboxyglutamic acid (Gla) domain binds C6PS only in the absence of Ca 2+ ( k
d â¼ 1 m m ), although this PS site does not influence the functional response of factor X a . Second, a Ca 2+ -dependent binding site is in the epidermal growth factor domains (EGF NC ) that are linked by Ca 2+ and C6PS binding to the Gla domain. This site appears to be the lipid regulatory site of factor X a . Third, a Ca 2+ -requiring site seems to be in the EGF C -catalytic domain. This site appears not to be a lipid regulatory site but rather to share residues with the substrate recognition
site. Finally, the full functional response to C6PS requires linkage of the Gla, EGF NC , and catalytic domains in the presence of Ca 2+ , meaning that PS regulation of factor X a involves linkage between widely separated parts of the protein. Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor Xa by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B. R. (1996) Biochemistry 35, 7482–7491). In the present study, we locate three C6PS binding sites to different domains of factor Xa using a combination of activity, circular dichroism, fluorescence, and equilibrium dialysis measurements on proteolytic and biosynthetic fragments of factor Xa. Our results demonstrate that the structural responses of human and bovine factor Xa to C6PS binding are somewhat different. Despite this difference, data obtained with fragments from both human and bovine factor Xa are consistent with a common hypothesis for the location of C6PS binding sites to different structural domains. First, the γ-carboxyglutamic acid (Gla) domain binds C6PS only in the absence of Ca2+ (kd ∼ 1 mm), although this PS site does not influence the functional response of factor Xa. Second, a Ca2+-dependent binding site is in the epidermal growth factor domains (EGFNC) that are linked by Ca2+ and C6PS binding to the Gla domain. This site appears to be the lipid regulatory site of factor Xa. Third, a Ca2+-requiring site seems to be in the EGFC-catalytic domain. This site appears not to be a lipid regulatory site but rather to share residues with the substrate recognition site. Finally, the full functional response to C6PS requires linkage of the Gla, EGFNC, and catalytic domains in the presence of Ca2+, meaning that PS regulation of factor Xa involves linkage between widely separated parts of the protein. Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor X(a) by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B. R. (1996) Biochemistry 35, 7482-7491). In the present study, we locate three C6PS binding sites to different domains of factor X(a) using a combination of activity, circular dichroism, fluorescence, and equilibrium dialysis measurements on proteolytic and biosynthetic fragments of factor X(a). Our results demonstrate that the structural responses of human and bovine factor X(a) to C6PS binding are somewhat different. Despite this difference, data obtained with fragments from both human and bovine factor X(a) are consistent with a common hypothesis for the location of C6PS binding sites to different structural domains. First, the gamma-carboxyglutamic acid (Gla) domain binds C6PS only in the absence of Ca(2+) (k(d) approximately 1 mm), although this PS site does not influence the functional response of factor X(a). Second, a Ca(2+)-dependent binding site is in the epidermal growth factor domains (EGF(NC)) that are linked by Ca(2+) and C6PS binding to the Gla domain. This site appears to be the lipid regulatory site of factor X(a). Third, a Ca(2+)-requiring site seems to be in the EGF(C)-catalytic domain. This site appears not to be a lipid regulatory site but rather to share residues with the substrate recognition site. Finally, the full functional response to C6PS requires linkage of the Gla, EGF(NC), and catalytic domains in the presence of Ca(2+), meaning that PS regulation of factor X(a) involves linkage between widely separated parts of the protein. |
Author | Wang, Jianfang Srivastava, Arvind Stenflo, Johan Esmon, Charles T. Majumder, Rinku Lentz, Barry R. Rezaie, Alireza R. |
Author_xml | – sequence: 1 givenname: Arvind surname: Srivastava fullname: Srivastava, Arvind organization: Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260 – sequence: 2 givenname: Jianfang surname: Wang fullname: Wang, Jianfang organization: Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260 – sequence: 3 givenname: Rinku surname: Majumder fullname: Majumder, Rinku organization: Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260 – sequence: 4 givenname: Alireza R. surname: Rezaie fullname: Rezaie, Alireza R. organization: Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, Missouri 63104 – sequence: 5 givenname: Johan surname: Stenflo fullname: Stenflo, Johan organization: Department of Clinical Chemistry, University of Lund, Malmö General Hospital, Malmö S214 01, Sweden – sequence: 6 givenname: Charles T. surname: Esmon fullname: Esmon, Charles T. organization: Department of Biochemistry and Biophysics and Pathology, Oklahoma Medical Research Foundation, University of Oklahoma Health Sciences Center and Howard Hughes Medical Institute, Oklahoma City, Oklahoma 73104 – sequence: 7 givenname: Barry R. surname: Lentz fullname: Lentz, Barry R. email: uncbrl@med.unc.edu organization: Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11707438$$D View this record in MEDLINE/PubMed |
BookMark | eNp1kEFLHDEUgIMoum579ShDD73NmpfMmMzR2toWVhS2BW8hk7xxIjPJmsy02F9vZBc8NZcQ-L5H3ndKDn3wSMgZ0BVQUV08tWZ1C7S-bASj9IAsgEpe8hoeDsmCUgZlw2p5Qk5TeqL5VA0ckxMAkWUuF2SzDkYP7p-eXPBF6Ir7PqRtn5_2ZUgYncfii_PW-cdi4yZMxRSKzRRnM81RD8XXMGrn05t5o80UYvGgP5CjTmf54_5ekt83335d_yjXd99_Xl-tS8MZoyUzlRasBQNcdkJwK5oGGs64qCSrq463FMFqyRGNBdE1DbV1Zw1WmlWyY3xJPu_mbmN4njFNanTJ4DBoj2FOSgC_FFXec0lWO9DEkFLETm2jG3V8UUDVW0aVM6r3jFk430-e2xHtO77vloFPO6B3j_1fF1G1LpgeR8WEUFyBrOsMyR2EOcIfh1El49AbtFkwk7LB_e8Dr43wjZ8 |
CitedBy_id | crossref_primary_10_1371_journal_pone_0135025 crossref_primary_10_1371_journal_pone_0161896 crossref_primary_10_1016_j_bbagen_2005_05_004 crossref_primary_10_1097_01_mbc_0000172832_65615_57 crossref_primary_10_1016_S0163_7827_03_00025_0 crossref_primary_10_1093_jb_mvi072 crossref_primary_10_1088_0953_8984_18_28_S09 crossref_primary_10_1042_BJ20141177 crossref_primary_10_1021_bi047962t crossref_primary_10_1021_bi900240g crossref_primary_10_1074_jbc_M202879200 crossref_primary_10_1111_j_1538_7836_2011_04300_x crossref_primary_10_1111_trf_17784 crossref_primary_10_1016_j_transci_2005_11_010 crossref_primary_10_1007_s00232_022_00265_7 crossref_primary_10_1016_j_bpj_2008_10_013 crossref_primary_10_1021_bi301239z crossref_primary_10_1042_BJ20131099 crossref_primary_10_1111_j_1537_2995_2005_00647_x crossref_primary_10_1074_jbc_M206746200 crossref_primary_10_1016_j_bpj_2015_08_051 crossref_primary_10_1002_rth2_12017 crossref_primary_10_1042_BJ20140130 crossref_primary_10_1529_biophysj_106_089078 crossref_primary_10_1021_bi047655n crossref_primary_10_1016_S0006_3495_03_74939_X crossref_primary_10_1161_01_ATV_0000031340_68494_34 crossref_primary_10_1371_journal_pone_0100006 crossref_primary_10_1182_blood_2015_03_636761 crossref_primary_10_1021_bi011844d crossref_primary_10_1021_bi801199v crossref_primary_10_1021_bi020017p crossref_primary_10_1021_bi051469f crossref_primary_10_1042_BSR20204077 crossref_primary_10_1074_jbc_M111_260141 crossref_primary_10_1074_jbc_M200893200 |
Cites_doi | 10.1073/pnas.95.12.6630 10.1016/S0021-9258(18)53078-7 10.1016/0003-9861(75)90106-X 10.1016/0076-6879(93)22027-D 10.1021/bi952063d 10.1021/bi9626160 10.1021/bi00556a006 10.1074/jbc.M001386200 10.1038/351164a0 10.1021/ac60119a033 10.1016/S0021-9258(18)41562-1 10.1016/S0076-6879(76)45016-4 10.1073/pnas.92.24.11185 10.1021/bi00638a007 10.1182/blood.V78.7.1637.1637 10.1111/j.1432-1033.1980.tb04458.x 10.1016/S0021-9258(19)49415-5 10.1016/S0076-6879(76)45014-0 10.1016/S0006-3495(97)78904-5 10.1002/prot.340070302 10.1016/S0021-9258(17)35615-6 10.1021/bi00480a023 10.1042/bj1310107 10.1074/jbc.271.39.23807 10.1016/0049-3848(85)90122-7 10.1016/S0021-9258(17)32918-6 10.1038/nsb0695-504 10.1074/jbc.272.35.22037 10.1021/bi00141a004 10.1055/s-0038-1649946 10.1021/bi9926781 10.1073/pnas.92.21.9796 10.1021/bi960633j 10.1006/abio.1996.0084 10.1016/S0021-9258(18)45150-2 10.1016/S0021-9258(19)81346-7 10.1074/jbc.271.47.29988 10.1016/S0021-9258(19)84792-0 10.1110/ps.9.3.619 10.1016/S0021-9258(18)47152-9 10.1006/abio.2000.4880 10.1021/bi992006a 10.1016/S0021-9258(18)52265-1 10.1006/jmbi.1993.1441 10.1016/S0021-9258(17)31831-8 10.1016/S0021-9258(19)47060-9 |
ContentType | Journal Article |
Copyright | 2002 © 2002 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. |
Copyright_xml | – notice: 2002 © 2002 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. |
DBID | 6I. AAFTH CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1074/jbc.M105697200 |
DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology Chemistry |
EISSN | 1083-351X |
EndPage | 1863 |
ExternalDocumentID | 10_1074_jbc_M105697200 11707438 277_3_1855 S0021925820878016 |
Genre | Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S Journal Article |
GrantInformation_xml | – fundername: NHLBI NIH HHS grantid: HL62565 – fundername: NHLBI NIH HHS grantid: HL45916 – fundername: NHLBI NIH HHS grantid: P01 HL54804 |
GroupedDBID | --- -DZ -ET -~X .55 .GJ 0SF 186 18M 2WC 34G 39C 3O- 53G 5BI 5GY 5RE 5VS 6I. 6TJ 79B 85S AAEDW AAFTH AAFWJ AARDX AAXUO ABDNZ ABFSI ABOCM ABPPZ ABRJW ABTAH ACGFO ACNCT ADBBV ADIYS ADNWM AENEX AEXQZ AFFNX AFMIJ AFOSN AFPKN AHPSJ AI. ALMA_UNASSIGNED_HOLDINGS BTFSW C1A CJ0 CS3 DIK DU5 E3Z EBS EJD F20 F5P FA8 FDB FRP GROUPED_DOAJ GX1 HH5 IH2 KQ8 L7B MVM N9A NHB OHT OK1 P-O P0W P2P R.V RHF RHI RNS ROL RPM SJN TBC TN5 TR2 UHB UKR UPT UQL VH1 VQA W8F WH7 WHG WOQ X7M XFK XSW Y6R YQT YSK YWH YYP YZZ ZA5 ZE2 ZGI ZY4 ~02 ~KM - 02 55 AAWZA ABFLS ABPTK ABUFD ABZEH ADACO ADBIT ADCOW AEILP AIZTS DL DZ ET FH7 GJ H13 KM LI MYA O0- X XHC 0R~ AALRI ADVLN AITUG AKRWK AMRAJ CGR CUY CVF ECM EIF NPM 29J 4.4 41~ AAYJJ AAYOK AAYXX ACSFO ACYGS AOIJS BAWUL CITATION E.L HYE J5H QZG XJT 7X8 |
ID | FETCH-LOGICAL-c3220-2c4a72b1c138f773d79919323748254f3b0e1da83eecd17f990d5fdce4a248f23 |
ISSN | 0021-9258 |
IngestDate | Fri Aug 16 03:59:35 EDT 2024 Fri Aug 23 01:51:57 EDT 2024 Sat Sep 28 08:30:20 EDT 2024 Tue Jan 05 14:52:14 EST 2021 Fri Feb 23 02:45:51 EST 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Language | English |
License | This is an open access article under the CC BY license. |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-c3220-2c4a72b1c138f773d79919323748254f3b0e1da83eecd17f990d5fdce4a248f23 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://dx.doi.org/10.1074/jbc.M105697200 |
PMID | 11707438 |
PQID | 71367474 |
PQPubID | 23479 |
PageCount | 9 |
ParticipantIDs | proquest_miscellaneous_71367474 crossref_primary_10_1074_jbc_M105697200 pubmed_primary_11707438 highwire_biochem_277_3_1855 elsevier_sciencedirect_doi_10_1074_jbc_M105697200 |
ProviderPackageCode | RHF RHI |
PublicationCentury | 2000 |
PublicationDate | 2002-01-18 |
PublicationDateYYYYMMDD | 2002-01-18 |
PublicationDate_xml | – month: 01 year: 2002 text: 2002-01-18 day: 18 |
PublicationDecade | 2000 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | The Journal of biological chemistry |
PublicationTitleAlternate | J Biol Chem |
PublicationYear | 2002 |
Publisher | Elsevier Inc American Society for Biochemistry and Molecular Biology |
Publisher_xml | – name: Elsevier Inc – name: American Society for Biochemistry and Molecular Biology |
References | Brandstetter, Bauer, Huber, Lollar, Bode (bib8) 1995; 92 Lim, Bloomfield, Nelsestuen (bib44) 1977; 16 Sunnerhagen, Olah, Stenflo, Forsen, Drakenberg, Trewhella (bib19) 1996; 35 Persson, Selander, Linse, Drakenberg, Ohlin, Stenflo (bib14) 1989; 264 Persson, Valcarce, Stenflo (bib25) 1991; 266 Dahlback, Stenflo (bib22) 1980; 104 Ullner, Selander, Persson, Stenflo, Drakenberg, Teleman (bib39) 1992; 31 Henriksen, Jackson (bib13) 1975; 170 Husten, Esmon, Johnson (bib37) 1987; 262 Chen, Toribara, Warner (bib38) 1956; 28 McDonald, Shah, Schwalbe, Kisiel, Dahlback, Nelsestuen (bib48) 1997; 36 Kamata, Kawamoto, Honma, Iwama, Kim (bib7) 1998; 95 Vindigni, Winfield, Ayala, Di Cera (bib28) 2000; 9 Koppaka, Wang, Banerjee, Lentz (bib1) 1996; 35 Handford, Mayhew, Baron, Winship, Campbell, Brownlee (bib12) 1991; 351 Guinto, Vindigni, Ayala, Dang, Di Cera (bib30) 1995; 92 Nossel (bib23) 1964; 12 Nelsestuen, Broderius, Martin (bib43) 1976; 251 Jameson, Roberts, Adams, Kyle, Elmore (bib24) 1973; 131 Stenflo (bib4) 1991; 78 Jesty, Nemerson (bib10) 1976; 45 Sandberg, Bode, Dombrose, Hoechli, Lentz (bib2) 1985; 39 Greenfield (bib32) 1996; 235 Rezaie, He (bib36) 2000; 39 Sreerama, Woody (bib33) 2000; 287 Lecompte, Miller (bib47) 1980; 19 Rezaie (bib29) 1996; 271 Schwalbe, Ryan, Stern, Kisiel, Dahlback, Nelsestuen (bib45) 1989; 264 Valcarce, Holmgren, Stenflo (bib18) 1994; 269 Morita, Jackson (bib27) 1986; 261 Rezaie, Esmon (bib15) 1994; 269 Mann (bib20) 1976; 45 Tendian, Lentz (bib21) 1990; 29 Persson, Hogg, Stenflo (bib17) 1993; 268 Underwood, Zhong, Mathur, Heyduk, Bajaj (bib35) 2000; 275 Brandstetter, Kuhne, Bode, Huber, von der Saal, Wirthensohn, Engh (bib6) 1996; 271 Sunnerhagen, Forsen, Hoffren, Drakenberg, Teleman, Stenflo (bib42) 1995; 2 Fujimura, Kambayash, Monden, Kato, Miyata (bib11) 1995; 74 Ellison, Castellino (bib31) 1997; 72 Valcarce, Persson, Astermark, Ohlin, Stenflo (bib26) 1993; 222 Johnson (bib34) 1990; 7 Sims, Faioni, Wiedmer, Shattil (bib3) 1988; 263 Padmanabhan, Padmanabhan, Tulinsky, Park, Bode, Huber, Blankenship, Cardin, Kisiel (bib5) 1993; 232 Monnaie, Arosio, Griffon, Rose, Rezaie, Di Cera (bib40) 2000; 39 Sabharwal, Padmanabhan, Tulinsky, Mathur, Gorka, Bajaj (bib9) 1997; 272 Pearce, Hof, Lentz, Thompson (bib46) 1993; 268 Rezaie, Neuenschwander, Morrissey, Esmon (bib16) 1993; 268 Rezaie (10.1074/jbc.M105697200_bib36) 2000; 39 Stenflo (10.1074/jbc.M105697200_bib4) 1991; 78 Rezaie (10.1074/jbc.M105697200_bib16) 1993; 268 Persson (10.1074/jbc.M105697200_bib17) 1993; 268 McDonald (10.1074/jbc.M105697200_bib48) 1997; 36 Jameson (10.1074/jbc.M105697200_bib24) 1973; 131 Jesty (10.1074/jbc.M105697200_bib10) 1976; 45 Johnson (10.1074/jbc.M105697200_bib34) 1990; 7 Husten (10.1074/jbc.M105697200_bib37) 1987; 262 Kamata (10.1074/jbc.M105697200_bib7) 1998; 95 Brandstetter (10.1074/jbc.M105697200_bib6) 1996; 271 Fujimura (10.1074/jbc.M105697200_bib11) 1995; 74 Persson (10.1074/jbc.M105697200_bib14) 1989; 264 Nelsestuen (10.1074/jbc.M105697200_bib43) 1976; 251 Sreerama (10.1074/jbc.M105697200_bib33) 2000; 287 Rezaie (10.1074/jbc.M105697200_bib15) 1994; 269 Sims (10.1074/jbc.M105697200_bib3) 1988; 263 Ellison (10.1074/jbc.M105697200_bib31) 1997; 72 Valcarce (10.1074/jbc.M105697200_bib18) 1994; 269 Dahlback (10.1074/jbc.M105697200_bib22) 1980; 104 Rezaie (10.1074/jbc.M105697200_bib29) 1996; 271 Sunnerhagen (10.1074/jbc.M105697200_bib42) 1995; 2 Tendian (10.1074/jbc.M105697200_bib21) 1990; 29 Pearce (10.1074/jbc.M105697200_bib46) 1993; 268 Koppaka (10.1074/jbc.M105697200_bib1) 1996; 35 Sandberg (10.1074/jbc.M105697200_bib2) 1985; 39 Mann (10.1074/jbc.M105697200_bib20) 1976; 45 Valcarce (10.1074/jbc.M105697200_bib26) 1993; 222 Sabharwal (10.1074/jbc.M105697200_bib9) 1997; 272 Chen (10.1074/jbc.M105697200_bib38) 1956; 28 Schwalbe (10.1074/jbc.M105697200_bib45) 1989; 264 Nossel (10.1074/jbc.M105697200_bib23) 1964; 12 Vindigni (10.1074/jbc.M105697200_bib28) 2000; 9 Underwood (10.1074/jbc.M105697200_bib35) 2000; 275 Lecompte (10.1074/jbc.M105697200_bib47) 1980; 19 Padmanabhan (10.1074/jbc.M105697200_bib5) 1993; 232 Sunnerhagen (10.1074/jbc.M105697200_bib19) 1996; 35 Monnaie (10.1074/jbc.M105697200_bib40) 2000; 39 10.1074/jbc.M105697200_bib41 Handford (10.1074/jbc.M105697200_bib12) 1991; 351 Greenfield (10.1074/jbc.M105697200_bib32) 1996; 235 Lim (10.1074/jbc.M105697200_bib44) 1977; 16 Brandstetter (10.1074/jbc.M105697200_bib8) 1995; 92 Morita (10.1074/jbc.M105697200_bib27) 1986; 261 Persson (10.1074/jbc.M105697200_bib25) 1991; 266 Henriksen (10.1074/jbc.M105697200_bib13) 1975; 170 Guinto (10.1074/jbc.M105697200_bib30) 1995; 92 Ullner (10.1074/jbc.M105697200_bib39) 1992; 31 |
References_xml | – volume: 12 start-page: 505 year: 1964 end-page: 518 ident: bib23 publication-title: Thromb. Diath. Haemorrh. contributor: fullname: Nossel – volume: 45 start-page: 95 year: 1976 end-page: 107 ident: bib10 publication-title: Methods Enzymol. contributor: fullname: Nemerson – volume: 269 start-page: 21495 year: 1994 end-page: 21499 ident: bib15 publication-title: J. Biol. Chem. contributor: fullname: Esmon – volume: 235 start-page: 1 year: 1996 end-page: 10 ident: bib32 publication-title: Anal. Biochem. contributor: fullname: Greenfield – volume: 39 start-page: 63 year: 1985 end-page: 79 ident: bib2 publication-title: Thromb. Res. contributor: fullname: Lentz – volume: 72 start-page: 2605 year: 1997 end-page: 2615 ident: bib31 publication-title: Biophys. J. contributor: fullname: Castellino – volume: 9 start-page: 619 year: 2000 end-page: 622 ident: bib28 publication-title: Protein Sci. contributor: fullname: Di Cera – volume: 45 start-page: 123 year: 1976 end-page: 156 ident: bib20 publication-title: Methods Enzymol. contributor: fullname: Mann – volume: 268 start-page: 8176 year: 1993 end-page: 8180 ident: bib16 publication-title: J. Biol. Chem. contributor: fullname: Esmon – volume: 287 start-page: 252 year: 2000 end-page: 260 ident: bib33 publication-title: Anal. Biochem. contributor: fullname: Woody – volume: 264 start-page: 20288 year: 1989 end-page: 20296 ident: bib45 publication-title: J. Biol. Chem. contributor: fullname: Nelsestuen – volume: 7 start-page: 205 year: 1990 end-page: 214 ident: bib34 publication-title: Proteins contributor: fullname: Johnson – volume: 2 start-page: 504 year: 1995 end-page: 509 ident: bib42 publication-title: Nat. Struct. Biol. contributor: fullname: Stenflo – volume: 35 start-page: 7482 year: 1996 end-page: 7491 ident: bib1 publication-title: Biochemistry contributor: fullname: Lentz – volume: 275 start-page: 36876 year: 2000 end-page: 36884 ident: bib35 publication-title: J. Biol. Chem. contributor: fullname: Bajaj – volume: 35 start-page: 11547 year: 1996 end-page: 11559 ident: bib19 publication-title: Biochemistry contributor: fullname: Trewhella – volume: 268 start-page: 22984 year: 1993 end-page: 22991 ident: bib46 publication-title: J. Biol. Chem. contributor: fullname: Thompson – volume: 131 start-page: 107 year: 1973 end-page: 117 ident: bib24 publication-title: Biochem. J. contributor: fullname: Elmore – volume: 74 start-page: 1381 year: 1995 end-page: 1382 ident: bib11 publication-title: Thromb. Haemost. contributor: fullname: Miyata – volume: 351 start-page: 164 year: 1991 end-page: 167 ident: bib12 publication-title: Nature contributor: fullname: Brownlee – volume: 28 start-page: 1756 year: 1956 end-page: 1758 ident: bib38 publication-title: Analyt. Chem. contributor: fullname: Warner – volume: 31 start-page: 5974 year: 1992 end-page: 5983 ident: bib39 publication-title: Biochemistry contributor: fullname: Teleman – volume: 29 start-page: 6720 year: 1990 end-page: 6729 ident: bib21 publication-title: Biochemistry contributor: fullname: Lentz – volume: 251 start-page: 6886 year: 1976 end-page: 6893 ident: bib43 publication-title: J. Biol. Chem. contributor: fullname: Martin – volume: 104 start-page: 549 year: 1980 end-page: 557 ident: bib22 publication-title: Eur. J. Biochem. contributor: fullname: Stenflo – volume: 92 start-page: 9796 year: 1995 end-page: 9800 ident: bib8 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Bode – volume: 268 start-page: 22531 year: 1993 end-page: 22539 ident: bib17 publication-title: J. Biol. Chem. contributor: fullname: Stenflo – volume: 269 start-page: 26011 year: 1994 end-page: 26016 ident: bib18 publication-title: J. Biol. Chem. contributor: fullname: Stenflo – volume: 263 start-page: 18205 year: 1988 end-page: 18212 ident: bib3 publication-title: J. Biol. Chem. contributor: fullname: Shattil – volume: 39 start-page: 5349 year: 2000 end-page: 5354 ident: bib40 publication-title: Biochemistry contributor: fullname: Di Cera – volume: 16 start-page: 4177 year: 1977 end-page: 4181 ident: bib44 publication-title: Biochemistry contributor: fullname: Nelsestuen – volume: 19 start-page: 3439 year: 1980 end-page: 3446 ident: bib47 publication-title: Biochemistry contributor: fullname: Miller – volume: 78 start-page: 1637 year: 1991 end-page: 1651 ident: bib4 publication-title: Blood contributor: fullname: Stenflo – volume: 170 start-page: 149 year: 1975 end-page: 159 ident: bib13 publication-title: Arch. Biochem. Biophys. contributor: fullname: Jackson – volume: 261 start-page: 4015 year: 1986 end-page: 4023 ident: bib27 publication-title: J. Biol. Chem. contributor: fullname: Jackson – volume: 271 start-page: 23807 year: 1996 end-page: 23814 ident: bib29 publication-title: J. Biol. Chem. contributor: fullname: Rezaie – volume: 92 start-page: 11185 year: 1995 end-page: 11189 ident: bib30 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Di Cera – volume: 262 start-page: 12953 year: 1987 end-page: 12961 ident: bib37 publication-title: J. Biol. Chem. contributor: fullname: Johnson – volume: 39 start-page: 1817 year: 2000 end-page: 1825 ident: bib36 publication-title: Biochemistry contributor: fullname: He – volume: 95 start-page: 6630 year: 1998 end-page: 6635 ident: bib7 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Kim – volume: 232 start-page: 947 year: 1993 end-page: 966 ident: bib5 publication-title: J. Mol. Biol. contributor: fullname: Kisiel – volume: 266 start-page: 2453 year: 1991 end-page: 2458 ident: bib25 publication-title: J. Biol. Chem. contributor: fullname: Stenflo – volume: 271 start-page: 29988 year: 1996 end-page: 29992 ident: bib6 publication-title: J. Biol. Chem. contributor: fullname: Engh – volume: 222 start-page: 416 year: 1993 end-page: 435 ident: bib26 publication-title: Methods Enzymol. contributor: fullname: Stenflo – volume: 272 start-page: 22037 year: 1997 end-page: 22045 ident: bib9 publication-title: J. Biol. Chem. contributor: fullname: Bajaj – volume: 264 start-page: 16897 year: 1989 end-page: 16904 ident: bib14 publication-title: J. Biol. Chem. contributor: fullname: Stenflo – volume: 36 start-page: 5120 year: 1997 end-page: 5127 ident: bib48 publication-title: Biochemistry contributor: fullname: Nelsestuen – volume: 95 start-page: 6630 year: 1998 ident: 10.1074/jbc.M105697200_bib7 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.95.12.6630 contributor: fullname: Kamata – volume: 268 start-page: 8176 year: 1993 ident: 10.1074/jbc.M105697200_bib16 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)53078-7 contributor: fullname: Rezaie – volume: 170 start-page: 149 year: 1975 ident: 10.1074/jbc.M105697200_bib13 publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(75)90106-X contributor: fullname: Henriksen – volume: 12 start-page: 505 year: 1964 ident: 10.1074/jbc.M105697200_bib23 publication-title: Thromb. Diath. Haemorrh. contributor: fullname: Nossel – volume: 222 start-page: 416 year: 1993 ident: 10.1074/jbc.M105697200_bib26 publication-title: Methods Enzymol. doi: 10.1016/0076-6879(93)22027-D contributor: fullname: Valcarce – volume: 35 start-page: 7482 year: 1996 ident: 10.1074/jbc.M105697200_bib1 publication-title: Biochemistry doi: 10.1021/bi952063d contributor: fullname: Koppaka – volume: 36 start-page: 5120 year: 1997 ident: 10.1074/jbc.M105697200_bib48 publication-title: Biochemistry doi: 10.1021/bi9626160 contributor: fullname: McDonald – volume: 19 start-page: 3439 year: 1980 ident: 10.1074/jbc.M105697200_bib47 publication-title: Biochemistry doi: 10.1021/bi00556a006 contributor: fullname: Lecompte – volume: 275 start-page: 36876 year: 2000 ident: 10.1074/jbc.M105697200_bib35 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M001386200 contributor: fullname: Underwood – volume: 351 start-page: 164 year: 1991 ident: 10.1074/jbc.M105697200_bib12 publication-title: Nature doi: 10.1038/351164a0 contributor: fullname: Handford – volume: 28 start-page: 1756 year: 1956 ident: 10.1074/jbc.M105697200_bib38 publication-title: Analyt. Chem. doi: 10.1021/ac60119a033 contributor: fullname: Chen – volume: 268 start-page: 22531 year: 1993 ident: 10.1074/jbc.M105697200_bib17 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)41562-1 contributor: fullname: Persson – volume: 45 start-page: 123 year: 1976 ident: 10.1074/jbc.M105697200_bib20 publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(76)45016-4 contributor: fullname: Mann – volume: 92 start-page: 11185 year: 1995 ident: 10.1074/jbc.M105697200_bib30 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.92.24.11185 contributor: fullname: Guinto – volume: 16 start-page: 4177 year: 1977 ident: 10.1074/jbc.M105697200_bib44 publication-title: Biochemistry doi: 10.1021/bi00638a007 contributor: fullname: Lim – volume: 78 start-page: 1637 year: 1991 ident: 10.1074/jbc.M105697200_bib4 publication-title: Blood doi: 10.1182/blood.V78.7.1637.1637 contributor: fullname: Stenflo – volume: 104 start-page: 549 year: 1980 ident: 10.1074/jbc.M105697200_bib22 publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1980.tb04458.x contributor: fullname: Dahlback – volume: 268 start-page: 22984 year: 1993 ident: 10.1074/jbc.M105697200_bib46 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)49415-5 contributor: fullname: Pearce – volume: 45 start-page: 95 year: 1976 ident: 10.1074/jbc.M105697200_bib10 publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(76)45014-0 contributor: fullname: Jesty – volume: 72 start-page: 2605 year: 1997 ident: 10.1074/jbc.M105697200_bib31 publication-title: Biophys. J. doi: 10.1016/S0006-3495(97)78904-5 contributor: fullname: Ellison – volume: 7 start-page: 205 year: 1990 ident: 10.1074/jbc.M105697200_bib34 publication-title: Proteins doi: 10.1002/prot.340070302 contributor: fullname: Johnson – ident: 10.1074/jbc.M105697200_bib41 – volume: 261 start-page: 4015 year: 1986 ident: 10.1074/jbc.M105697200_bib27 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35615-6 contributor: fullname: Morita – volume: 29 start-page: 6720 year: 1990 ident: 10.1074/jbc.M105697200_bib21 publication-title: Biochemistry doi: 10.1021/bi00480a023 contributor: fullname: Tendian – volume: 131 start-page: 107 year: 1973 ident: 10.1074/jbc.M105697200_bib24 publication-title: Biochem. J. doi: 10.1042/bj1310107 contributor: fullname: Jameson – volume: 271 start-page: 23807 year: 1996 ident: 10.1074/jbc.M105697200_bib29 publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.39.23807 contributor: fullname: Rezaie – volume: 39 start-page: 63 year: 1985 ident: 10.1074/jbc.M105697200_bib2 publication-title: Thromb. Res. doi: 10.1016/0049-3848(85)90122-7 contributor: fullname: Sandberg – volume: 251 start-page: 6886 year: 1976 ident: 10.1074/jbc.M105697200_bib43 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)32918-6 contributor: fullname: Nelsestuen – volume: 2 start-page: 504 year: 1995 ident: 10.1074/jbc.M105697200_bib42 publication-title: Nat. Struct. Biol. doi: 10.1038/nsb0695-504 contributor: fullname: Sunnerhagen – volume: 272 start-page: 22037 year: 1997 ident: 10.1074/jbc.M105697200_bib9 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.35.22037 contributor: fullname: Sabharwal – volume: 31 start-page: 5974 year: 1992 ident: 10.1074/jbc.M105697200_bib39 publication-title: Biochemistry doi: 10.1021/bi00141a004 contributor: fullname: Ullner – volume: 74 start-page: 1381 year: 1995 ident: 10.1074/jbc.M105697200_bib11 publication-title: Thromb. Haemost. doi: 10.1055/s-0038-1649946 contributor: fullname: Fujimura – volume: 39 start-page: 5349 year: 2000 ident: 10.1074/jbc.M105697200_bib40 publication-title: Biochemistry doi: 10.1021/bi9926781 contributor: fullname: Monnaie – volume: 92 start-page: 9796 year: 1995 ident: 10.1074/jbc.M105697200_bib8 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.92.21.9796 contributor: fullname: Brandstetter – volume: 35 start-page: 11547 year: 1996 ident: 10.1074/jbc.M105697200_bib19 publication-title: Biochemistry doi: 10.1021/bi960633j contributor: fullname: Sunnerhagen – volume: 235 start-page: 1 year: 1996 ident: 10.1074/jbc.M105697200_bib32 publication-title: Anal. Biochem. doi: 10.1006/abio.1996.0084 contributor: fullname: Greenfield – volume: 262 start-page: 12953 year: 1987 ident: 10.1074/jbc.M105697200_bib37 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)45150-2 contributor: fullname: Husten – volume: 263 start-page: 18205 year: 1988 ident: 10.1074/jbc.M105697200_bib3 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)81346-7 contributor: fullname: Sims – volume: 271 start-page: 29988 year: 1996 ident: 10.1074/jbc.M105697200_bib6 publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.47.29988 contributor: fullname: Brandstetter – volume: 264 start-page: 16897 year: 1989 ident: 10.1074/jbc.M105697200_bib14 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)84792-0 contributor: fullname: Persson – volume: 9 start-page: 619 year: 2000 ident: 10.1074/jbc.M105697200_bib28 publication-title: Protein Sci. doi: 10.1110/ps.9.3.619 contributor: fullname: Vindigni – volume: 269 start-page: 26011 year: 1994 ident: 10.1074/jbc.M105697200_bib18 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47152-9 contributor: fullname: Valcarce – volume: 287 start-page: 252 year: 2000 ident: 10.1074/jbc.M105697200_bib33 publication-title: Anal. Biochem. doi: 10.1006/abio.2000.4880 contributor: fullname: Sreerama – volume: 39 start-page: 1817 year: 2000 ident: 10.1074/jbc.M105697200_bib36 publication-title: Biochemistry doi: 10.1021/bi992006a contributor: fullname: Rezaie – volume: 266 start-page: 2453 year: 1991 ident: 10.1074/jbc.M105697200_bib25 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)52265-1 contributor: fullname: Persson – volume: 232 start-page: 947 year: 1993 ident: 10.1074/jbc.M105697200_bib5 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1993.1441 contributor: fullname: Padmanabhan – volume: 269 start-page: 21495 year: 1994 ident: 10.1074/jbc.M105697200_bib15 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)31831-8 contributor: fullname: Rezaie – volume: 264 start-page: 20288 year: 1989 ident: 10.1074/jbc.M105697200_bib45 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)47060-9 contributor: fullname: Schwalbe |
SSID | ssj0000491 |
Score | 1.8904753 |
Snippet | Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor Xa by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B.... Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor X a by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz, B.... Binding of short chain phosphatidylserine (C6PS) enhances the proteolytic activity of factor X(a) by 60-fold (Koppaka, V., Wang, J., Banerjee, M., and Lentz,... |
SourceID | proquest crossref pubmed highwire elsevier |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 1855 |
SubjectTerms | Amides - metabolism Animals Binding Sites Cattle Circular Dichroism Factor Xa - chemistry Factor Xa - metabolism Humans Hydrolysis Phosphatidylserines - metabolism Protein Conformation Spectrometry, Fluorescence |
Title | Localization of Phosphatidylserine Binding Sites to Structural Domains of Factor Xa |
URI | https://dx.doi.org/10.1074/jbc.M105697200 http://www.jbc.org/content/277/3/1855.abstract https://www.ncbi.nlm.nih.gov/pubmed/11707438 https://search.proquest.com/docview/71367474 |
Volume | 277 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1db9MwFLXKeIAXBBuwMj78gOChSmkSp04fu8E0DYoE3UTfLMextcCaVDSttP5IfhPXH_kYrAh4idpISdyc0-vj5N5zEXo5FCQQMuReFCmpS3JSTy8jPJWGSRJLoUZCFydPPg5PzsnpLJp1Oj9aWUurMumLzY11Jf-DKuwDXHWV7D8gW58UdsBnwBe2gDBs_wrjD3oicoWUJpntolguLuBrenW5NHV9vcPMlq1Ms9KaOUyNYawx23hbzHlm0-COTdud3oy3xWpTNmYEq_Vrso4iVZu4hi_rTOeAfs_WHPTmug72p0A_xWEAX7ibI41jdv5t1Zvwr6t52mQHjy8h_G5473MfQN_wTF57IqFTOzwXRJsiAB2dWnmnh1lRD82mkFTdf13TzXbgM2kjgbV070sbmEEq6qqDWTtyB64DTNZe2Zs4DCokunGCAMWkJ4hE9CegLIcjao1SyxZbFnNDF92SB-RV3EyUVXLAL_NnndUIw2Eh05e-hW4HdBTphwHvPzXu9bAasx0c3e-rTEQpeXN9RNrK1l1-m16q7ay3L42MRDq7j-45quCxJeoD1JH5Ltob57ws5lf4FTbZxgaFXXTnqMJpD03bPMaFwr_zGDseY8NjXBa44TF2PNZHWh7jGX-Izo_fnR2deK7ZhydgThl4gSCcBokv_DBWlIYphZULLC60PVIQERUmA-mnPA6lFKlPFaioNFKpkIQHJFZB-Ajt5EUu97UNASdRGI0kVTGRsRrJdDAUEHeo8nkg_C56Xd1StrCeLszkYlDCAAfW4NBFfnXHmVOkVmky4NPWYw4qaFhiWc8aZnTRiwotBndZv53juSxWS0a1eSKhpIseWxCbsTkqPPnjmQ_Q3ebP-BTtAAryGQjmMnluWPgTCW3D2Q |
link.rule.ids | 315,786,790,27957,27958 |
linkProvider | Colorado Alliance of Research Libraries |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Localization+of+Phosphatidylserine+Binding+Sites+to+Structural+Domains+of+Factor+Xa&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=Arvind+Srivastava&rft.au=Jianfang+Wang&rft.au=Rinku+Majumder&rft.au=Alireza+R.+Rezaie&rft.date=2002-01-18&rft.pub=American+Society+for+Biochemistry+and+Molecular+Biology&rft.issn=0021-9258&rft.eissn=1083-351X&rft.volume=277&rft.issue=3&rft.spage=1855&rft_id=info:doi/10.1074%2Fjbc.M105697200&rft_id=info%3Apmid%2F11707438&rft.externalDBID=n%2Fa&rft.externalDocID=277_3_1855 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon |