Independent Interactions of Ubiquitin-Binding Domains in a Ubiquitin-Mediated Ternary Complex
Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface. We report the nuclear magnetic resonance (NMR) solution structures of the A20-like zinc finger (A20 Znf) UBD of the Ub receptor ZNF216, and i...
Saved in:
Published in | Biochemistry (Easton) Vol. 50; no. 42; pp. 9076 - 9087 |
---|---|
Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
25.10.2011
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface. We report the nuclear magnetic resonance (NMR) solution structures of the A20-like zinc finger (A20 Znf) UBD of the Ub receptor ZNF216, and its complex with Ub, and show that the binding surface on Ub centered on Asp58 leaves the canonical hydrophobic Ile44 patch free to participate in additional interactions. We have modeled ternary complexes of the different families of UBDs and show that while many are expected to bind competitively to the same Ile44 surface or show steric incompatibility, other combinations (in particular, those involving the A20 Znf domain) are consistent with a single Ub moiety simultaneously participating in multiple interactions with different UBDs. We subsequently demonstrate by NMR that the A20 Znf domain of ZNF216 and the UBA domain of the p62 protein (an Ile44-binding UBD), which function in the same biological pathways, are able to form such a Ub-mediated ternary complex through independent interactions with a single Ub. This work supports an emerging concept of Ub acting as a scaffold to mediate multiprotein complex assembly. |
---|---|
AbstractList | Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface. We report the nuclear magnetic resonance (NMR) solution structures of the A20-like zinc finger (A20 Znf) UBD of the Ub receptor ZNF216, and its complex with Ub, and show that the binding surface on Ub centered on Asp58 leaves the canonical hydrophobic Ile44 patch free to participate in additional interactions. We have modeled ternary complexes of the different families of UBDs and show that while many are expected to bind competitively to the same Ile44 surface or show steric incompatibility, other combinations (in particular, those involving the A20 Znf domain) are consistent with a single Ub moiety simultaneously participating in multiple interactions with different UBDs. We subsequently demonstrate by NMR that the A20 Znf domain of ZNF216 and the UBA domain of the p62 protein (an Ile44-binding UBD), which function in the same biological pathways, are able to form such a Ub-mediated ternary complex through independent interactions with a single Ub. This work supports an emerging concept of Ub acting as a scaffold to mediate multiprotein complex assembly. |
Author | Long, Jed E Layfield, Robert Strachan, Joanna Cavey, James R Shaw, Barry Searle, Mark S Garner, Thomas P Shedden, Elizabeth C |
AuthorAffiliation | University of Nottingham |
AuthorAffiliation_xml | – name: University of Nottingham |
Author_xml | – sequence: 1 givenname: Thomas P surname: Garner fullname: Garner, Thomas P – sequence: 2 givenname: Joanna surname: Strachan fullname: Strachan, Joanna – sequence: 3 givenname: Elizabeth C surname: Shedden fullname: Shedden, Elizabeth C – sequence: 4 givenname: Jed E surname: Long fullname: Long, Jed E – sequence: 5 givenname: James R surname: Cavey fullname: Cavey, James R – sequence: 6 givenname: Barry surname: Shaw fullname: Shaw, Barry – sequence: 7 givenname: Robert surname: Layfield fullname: Layfield, Robert – sequence: 8 givenname: Mark S surname: Searle fullname: Searle, Mark S email: mark.searle@nottingham.ac.uk |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21923101$$D View this record in MEDLINE/PubMed |
BookMark | eNptkE1LxDAQhoOsuB968A9ILyIeqpP0M0ddvxZWvOwepSTNVLK0SbdpQf-9kV0XD15mGObhZeaZkpGxBgk5p3BDgdFbqRlQGmV4RCY0YRDGnCcjMgGANGQ8hTGZOrfxYwxZfELGjHIWUaAT8r4wClv0xfTBwvTYibLX1rjAVsFa6u2ge23Ce22UNh_Bg22E9kttAvFn_YpKix5VsMLOiO4rmNumrfHzlBxXonZ4tu8zsn56XM1fwuXb82J-twxFlEMfKkFTEaVxzkGVmUihkjRN4jRJBMQJlBFnyACSGDOpMikkVgnPVSVyyco8k9GMXO1y285uB3R90WhXYl0Lg3ZwBfciWJwx7snrHVl21rkOq6LtdONPLigUPzKLg0zPXuxTB9mgOpC_9jxwuQNE6YqNHfzvtfsn6BtDUH0J |
CitedBy_id | crossref_primary_10_1002_pro_2195 crossref_primary_10_1002_ange_202006260 crossref_primary_10_1073_pnas_1809934115 crossref_primary_10_1002_anie_202110223 crossref_primary_10_1534_g3_115_017699 crossref_primary_10_1074_jbc_M113_486845 crossref_primary_10_18632_oncotarget_12509 crossref_primary_10_1093_nar_gkt470 crossref_primary_10_1016_j_febslet_2012_04_053 crossref_primary_10_1002_ange_202110223 crossref_primary_10_1002_pep2_24091 crossref_primary_10_1021_bi300058m crossref_primary_10_1021_bi401436h crossref_primary_10_1002_1873_3468_14951 crossref_primary_10_1002_anie_202006260 crossref_primary_10_1021_pr201167n crossref_primary_10_1074_jbc_M113_529032 crossref_primary_10_1002_prot_25535 crossref_primary_10_1016_j_biocel_2013_05_031 crossref_primary_10_1002_pmic_201600067 crossref_primary_10_3390_ijms21093036 crossref_primary_10_1371_journal_pcbi_1005319 crossref_primary_10_1002_pmic_201400341 crossref_primary_10_1042_BST20110729 crossref_primary_10_1016_j_febslet_2012_10_011 crossref_primary_10_1021_ja300749d crossref_primary_10_1021_ja210238g crossref_primary_10_1111_febs_16101 crossref_primary_10_3389_fonc_2022_955670 |
Cites_doi | 10.1016/0263-7855(96)00009-4 10.1038/ncb0805-758 10.1016/j.cell.2006.02.020 10.1002/prot.20449 10.1023/A:1011206132740 10.1016/j.molcel.2005.05.013 10.1016/j.molcel.2010.10.009 10.1073/pnas.95.11.5857 10.1023/A:1012998006281 10.1038/sj.emboj.7600945 10.1038/nature07254 10.1093/nar/25.24.4876 10.1093/emboj/18.11.3044 10.1038/nsmb1064 10.1038/nature02914 10.1038/sj.emboj.7600797 10.1038/nrm1960 10.1093/nar/gkp1016 10.1093/protein/2.1.27 10.1038/nrm2767 10.1080/10799890500240781 10.1016/j.molcel.2009.12.038 10.1016/j.bbadis.2008.10.011 10.1038/sj.embor.7400901 10.1359/jbmr.081204 10.1016/j.bbamem.2007.08.010 10.1023/A:1013336502594 10.1016/j.molcel.2009.06.010 10.1042/BST0370937 10.1016/j.jmb.2009.11.032 10.2353/ajpath.2006.050960 10.1186/1747-1028-2-11 10.1021/ja026939x 10.1128/MCB.24.18.8055-8068.2004 10.1021/bi00449a003 10.1016/j.cell.2006.03.009 10.1016/j.molcel.2010.05.003 10.1073/pnas.0906966106 10.1074/jbc.M400023200 10.1074/jbc.M309491200 10.1002/prot.21165 10.1016/j.febslet.2006.12.027 10.1126/science.1157092 10.1093/jn/129.1.227S 10.1093/nar/gkn664 10.1093/emboj/19.7.1576 10.1093/nar/gkm328 10.1038/nature06924 10.1073/pnas.0912335107 10.1016/S1090-7807(02)00014-9 10.1074/jbc.M704973200 10.1002/rcm.3232 10.1021/ja0574825 10.1093/nar/gkn305 10.1016/j.jmb.2007.03.008 10.1016/j.molcel.2009.01.014 10.1021/ac050511+ 10.1016/j.molcel.2009.11.012 10.1016/j.jmb.2007.12.029 10.1016/0014-5793(88)80559-3 10.1006/jmre.1998.1361 10.1038/nature07961 |
ContentType | Journal Article |
Copyright | Copyright © 2011 American Chemical Society |
Copyright_xml | – notice: Copyright © 2011 American Chemical Society |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1021/bi201137e |
DatabaseName | 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 | 1520-4995 |
EndPage | 9087 |
ExternalDocumentID | 10_1021_bi201137e 21923101 d108631885 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GrantInformation | We thank the EPSRC and BBSRC of the United Kingdom for providing funding and the University of Nottingham for support for core instrumentation. |
GrantInformation_xml | – fundername: Biotechnology and Biological Sciences Research Council |
GroupedDBID | - .K2 02 23N 3O- 4.4 53G 55 55A 5GY 5RE 5VS 7~N 85S AABXI ABFLS ABMVS ABOCM ABPTK ABUCX ABUFD ACGFS ACJ ACNCT ACS AEESW AENEX AFEFF AJYGW ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH CS3 D0L DU5 DZ EBS ED ED~ EJD F5P GNL IH9 IHE JG JG~ K2 KM L7B LG6 P2P ROL TN5 UI2 VF5 VG9 VQA W1F WH7 X X7M YZZ ZA5 --- -DZ -~X .55 ABJNI ABQRX ADHLV AGXLV AHGAQ CGR CUPRZ CUY CVF ECM EIF GGK NPM XSW ZCA ~02 ~KM AAYXX CITATION 7X8 |
ID | FETCH-LOGICAL-a380t-da16a364890dc7a60fb1654655a0450c392e20054e7bd7babef598dfa8b2c87b3 |
IEDL.DBID | ACS |
ISSN | 0006-2960 |
IngestDate | Sat Aug 17 01:43:16 EDT 2024 Fri Aug 23 01:45:09 EDT 2024 Sat Sep 28 08:30:12 EDT 2024 Thu Aug 27 13:41:58 EDT 2020 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 42 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a380t-da16a364890dc7a60fb1654655a0450c392e20054e7bd7babef598dfa8b2c87b3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 21923101 |
PQID | 900624729 |
PQPubID | 23479 |
PageCount | 12 |
ParticipantIDs | proquest_miscellaneous_900624729 crossref_primary_10_1021_bi201137e pubmed_primary_21923101 acs_journals_10_1021_bi201137e |
ProviderPackageCode | JG~ 55A AABXI GNL VF5 7~N ACJ VG9 W1F ACS AEESW AFEFF .K2 ABMVS ABUCX IH9 BAANH AQSVZ ED~ UI2 |
PublicationCentury | 2000 |
PublicationDate | 2011-10-25 |
PublicationDateYYYYMMDD | 2011-10-25 |
PublicationDate_xml | – month: 10 year: 2011 text: 2011-10-25 day: 25 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Biochemistry (Easton) |
PublicationTitleAlternate | Biochemistry |
PublicationYear | 2011 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | Yip K. H. M. (ref54/cit54) 2006; 169 Hierro A. (ref64/cit64) 2004; 431 The UniProt Consortium (ref24/cit24) 2009; 37 Hishiya A. (ref12/cit12) 2006; 25 Sanz L. (ref20/cit20) 1999; 18 Thompson J. D. (ref23/cit23) 1997; 25 Dominguez C. (ref43/cit43) 2003; 125 Komander D. (ref1/cit1) 2009; 37 Gould C. M. (ref26/cit26) 2010; 38 Siebenhener M. L. (ref53/cit53) 2004; 24 Kang Y. (ref57/cit57) 2007; 369 Ottiger M. (ref28/cit28) 1998; 131 Wu Y. (ref33/cit33) 2007; 1768 Huang J. (ref16/cit16) 2004; 279 Woelk T. (ref63/cit63) 2007; 2 Varadan R. (ref55/cit55) 2005; 18 Schreiner P. (ref59/cit59) 2008; 453 Lange O. F. (ref50/cit50) 2008; 320 Winget J. M. (ref7/cit7) 2010; 38 Lee S. (ref9/cit9) 2006; 13 Trempe J. F. (ref56/cit56) 2005; 24 Bosanac I. (ref49/cit49) 2010; 40 Seibenhener M. L. (ref52/cit52) 2007; 581 Kaltashov I. A. (ref47/cit47) 2005; 77 Sass H. J. (ref35/cit35) 2001; 21 Dosset P. (ref36/cit36) 2001; 20 Schwieters C. D. (ref37/cit37) 2003; 160 Nilges M. (ref39/cit39) 1988; 2 Sato Y. (ref11/cit11) 2008; 455 Bomar M. G. (ref6/cit6) 2010; 37 Otting G. (ref31/cit31) 1989; 85 Zhang D. (ref60/cit60) 2009; 36 Long J. (ref21/cit21) 2008; 283 Włodarski T. (ref51/cit51) 2009; 106 Vranken W. F. (ref27/cit27) 2005; 59 Hishiya A. (ref15/cit15) 2005; 25 Chen Z. J. (ref17/cit17) 2005; 7 Murton A. J. (ref14/cit14) 2008; 1782 Long J. (ref18/cit18) 2010; 396 Nilges M. (ref38/cit38) 1988; 239 Veros C. T. (ref46/cit46) 2007; 21 Seet B. T. (ref2/cit2) 2006; 7 Hubbard S. J. (ref44/cit44) 1993 Harper J. W. (ref5/cit5) 2006; 124 Hagai T. (ref3/cit3) 2010; 107 Raiborg C. (ref61/cit61) 2009; 458 Bomar M. G. (ref45/cit45) 2007; 8 Najat D. (ref65/cit65) 2009; 24 Lecker S. H. (ref13/cit13) 1999; 129 Sanz L. (ref19/cit19) 2000; 19 Bhattacharya A. (ref40/cit40) 2007; 66 Schwieters C. D. (ref48/cit48) 2003; 160 Wishart D. S. (ref42/cit42) 2008; 36 Dikic I. (ref4/cit4) 2009; 10 Schultz J. (ref25/cit25) 1998; 95 Berjanskii M. V. (ref34/cit34) 2007; 35 Penengo L. (ref10/cit10) 2006; 124 Chou J. J. (ref29/cit29) 2001; 21 Zhang D. (ref22/cit22) 2008; 377 Liang B. (ref32/cit32) 2006; 128 Chen Z. J. (ref8/cit8) 2009; 33 Koradi R. (ref41/cit41) 1996; 14 Teo H. (ref62/cit62) 2004; 279 Zhang D. (ref58/cit58) 2009; 35 Kay L. E. (ref30/cit30) 1989; 28 |
References_xml | – volume: 14 start-page: 51 year: 1996 ident: ref41/cit41 publication-title: J. Mol. Graphics doi: 10.1016/0263-7855(96)00009-4 contributor: fullname: Koradi R. – volume: 7 start-page: 758 year: 2005 ident: ref17/cit17 publication-title: Nat. Cell Biol. doi: 10.1038/ncb0805-758 contributor: fullname: Chen Z. J. – volume: 124 start-page: 1183 year: 2006 ident: ref10/cit10 publication-title: Cell doi: 10.1016/j.cell.2006.02.020 contributor: fullname: Penengo L. – volume: 59 start-page: 687 year: 2005 ident: ref27/cit27 publication-title: Proteins: Struct., Funct., Bioinf. doi: 10.1002/prot.20449 contributor: fullname: Vranken W. F. – volume: 20 start-page: 223 year: 2001 ident: ref36/cit36 publication-title: J. Biomol. NMR doi: 10.1023/A:1011206132740 contributor: fullname: Dosset P. – volume: 18 start-page: 687 year: 2005 ident: ref55/cit55 publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.05.013 contributor: fullname: Varadan R. – volume: 40 start-page: 548 year: 2010 ident: ref49/cit49 publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.10.009 contributor: fullname: Bosanac I. – volume: 95 start-page: 5857 year: 1998 ident: ref25/cit25 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.95.11.5857 contributor: fullname: Schultz J. – volume: 21 start-page: 275 year: 2001 ident: ref35/cit35 publication-title: J. Biomol. NMR doi: 10.1023/A:1012998006281 contributor: fullname: Sass H. J. – volume: 25 start-page: 554 year: 2006 ident: ref12/cit12 publication-title: EMBO J. doi: 10.1038/sj.emboj.7600945 contributor: fullname: Hishiya A. – volume: 455 start-page: 358 year: 2008 ident: ref11/cit11 publication-title: Nature doi: 10.1038/nature07254 contributor: fullname: Sato Y. – volume: 85 start-page: 586 year: 1989 ident: ref31/cit31 publication-title: J. Magn. Reson. contributor: fullname: Otting G. – volume: 25 start-page: 4876 year: 1997 ident: ref23/cit23 publication-title: Nucleic Acids Res. doi: 10.1093/nar/25.24.4876 contributor: fullname: Thompson J. D. – volume: 18 start-page: 3044 year: 1999 ident: ref20/cit20 publication-title: EMBO J. doi: 10.1093/emboj/18.11.3044 contributor: fullname: Sanz L. – volume: 13 start-page: 264 year: 2006 ident: ref9/cit9 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb1064 contributor: fullname: Lee S. – volume: 431 start-page: 221 year: 2004 ident: ref64/cit64 publication-title: Nature doi: 10.1038/nature02914 contributor: fullname: Hierro A. – volume-title: NACCESS year: 1993 ident: ref44/cit44 contributor: fullname: Hubbard S. J. – volume: 24 start-page: 3178 year: 2005 ident: ref56/cit56 publication-title: EMBO J. doi: 10.1038/sj.emboj.7600797 contributor: fullname: Trempe J. F. – volume: 7 start-page: 473 year: 2006 ident: ref2/cit2 publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1960 contributor: fullname: Seet B. T. – volume: 38 start-page: D167 year: 2010 ident: ref26/cit26 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkp1016 contributor: fullname: Gould C. M. – volume: 2 start-page: 27 year: 1988 ident: ref39/cit39 publication-title: Protein Eng. doi: 10.1093/protein/2.1.27 contributor: fullname: Nilges M. – volume: 10 start-page: 659 year: 2009 ident: ref4/cit4 publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2767 contributor: fullname: Dikic I. – volume: 25 start-page: 199 year: 2005 ident: ref15/cit15 publication-title: J. Recept. Signal Transduction Res. doi: 10.1080/10799890500240781 contributor: fullname: Hishiya A. – volume: 37 start-page: 408 year: 2010 ident: ref6/cit6 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.12.038 contributor: fullname: Bomar M. G. – volume: 1782 start-page: 730 year: 2008 ident: ref14/cit14 publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2008.10.011 contributor: fullname: Murton A. J. – volume: 8 start-page: 247 year: 2007 ident: ref45/cit45 publication-title: EMBO Rep. doi: 10.1038/sj.embor.7400901 contributor: fullname: Bomar M. G. – volume: 24 start-page: 632 year: 2009 ident: ref65/cit65 publication-title: J. Bone Miner. Res. doi: 10.1359/jbmr.081204 contributor: fullname: Najat D. – volume: 1768 start-page: 3206 year: 2007 ident: ref33/cit33 publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamem.2007.08.010 contributor: fullname: Wu Y. – volume: 21 start-page: 377 year: 2001 ident: ref29/cit29 publication-title: J. Biomol. NMR doi: 10.1023/A:1013336502594 contributor: fullname: Chou J. J. – volume: 35 start-page: 280 year: 2009 ident: ref58/cit58 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.06.010 contributor: fullname: Zhang D. – volume: 37 start-page: 937 year: 2009 ident: ref1/cit1 publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0370937 contributor: fullname: Komander D. – volume: 396 start-page: 178 year: 2010 ident: ref18/cit18 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2009.11.032 contributor: fullname: Long J. – volume: 169 start-page: 503 year: 2006 ident: ref54/cit54 publication-title: Am. J. Pathol. doi: 10.2353/ajpath.2006.050960 contributor: fullname: Yip K. H. M. – volume: 2 start-page: 11 year: 2007 ident: ref63/cit63 publication-title: Cell Div. doi: 10.1186/1747-1028-2-11 contributor: fullname: Woelk T. – volume: 125 start-page: 1731 year: 2003 ident: ref43/cit43 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja026939x contributor: fullname: Dominguez C. – volume: 24 start-page: 8055 year: 2004 ident: ref53/cit53 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.18.8055-8068.2004 contributor: fullname: Siebenhener M. L. – volume: 28 start-page: 8972 year: 1989 ident: ref30/cit30 publication-title: Biochemistry doi: 10.1021/bi00449a003 contributor: fullname: Kay L. E. – volume: 124 start-page: 1133 year: 2006 ident: ref5/cit5 publication-title: Cell doi: 10.1016/j.cell.2006.03.009 contributor: fullname: Harper J. W. – volume: 38 start-page: 627 year: 2010 ident: ref7/cit7 publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.05.003 contributor: fullname: Winget J. M. – volume: 106 start-page: 19346 year: 2009 ident: ref51/cit51 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0906966106 contributor: fullname: Włodarski T. – volume: 279 start-page: 28689 year: 2004 ident: ref62/cit62 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M400023200 contributor: fullname: Teo H. – volume: 279 start-page: 16847 year: 2004 ident: ref16/cit16 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M309491200 contributor: fullname: Huang J. – volume: 66 start-page: 778 year: 2007 ident: ref40/cit40 publication-title: Proteins doi: 10.1002/prot.21165 contributor: fullname: Bhattacharya A. – volume: 581 start-page: 175 year: 2007 ident: ref52/cit52 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2006.12.027 contributor: fullname: Seibenhener M. L. – volume: 320 start-page: 1471 year: 2008 ident: ref50/cit50 publication-title: Science doi: 10.1126/science.1157092 contributor: fullname: Lange O. F. – volume: 129 start-page: 227S year: 1999 ident: ref13/cit13 publication-title: J. Nutr. doi: 10.1093/jn/129.1.227S contributor: fullname: Lecker S. H. – volume: 37 start-page: D169 year: 2009 ident: ref24/cit24 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn664 contributor: fullname: The UniProt Consortium – volume: 19 start-page: 1576 year: 2000 ident: ref19/cit19 publication-title: EMBO J. doi: 10.1093/emboj/19.7.1576 contributor: fullname: Sanz L. – volume: 35 start-page: W531 year: 2007 ident: ref34/cit34 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkm328 contributor: fullname: Berjanskii M. V. – volume: 453 start-page: 548 year: 2008 ident: ref59/cit59 publication-title: Nature doi: 10.1038/nature06924 contributor: fullname: Schreiner P. – volume: 107 start-page: 2001 year: 2010 ident: ref3/cit3 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0912335107 contributor: fullname: Hagai T. – volume: 160 start-page: 65 year: 2003 ident: ref48/cit48 publication-title: J. Magn. Reson. doi: 10.1016/S1090-7807(02)00014-9 contributor: fullname: Schwieters C. D. – volume: 283 start-page: 5427 year: 2008 ident: ref21/cit21 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M704973200 contributor: fullname: Long J. – volume: 21 start-page: 3505 year: 2007 ident: ref46/cit46 publication-title: Rapid Commun. Mass Spectrom. doi: 10.1002/rcm.3232 contributor: fullname: Veros C. T. – volume: 128 start-page: 4389 year: 2006 ident: ref32/cit32 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0574825 contributor: fullname: Liang B. – volume: 36 start-page: W496 year: 2008 ident: ref42/cit42 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn305 contributor: fullname: Wishart D. S. – volume: 369 start-page: 168 year: 2007 ident: ref57/cit57 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.03.008 contributor: fullname: Kang Y. – volume: 33 start-page: 275 year: 2009 ident: ref8/cit8 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.01.014 contributor: fullname: Chen Z. J. – volume: 77 start-page: 5370 year: 2005 ident: ref47/cit47 publication-title: Anal. Chem. doi: 10.1021/ac050511+ contributor: fullname: Kaltashov I. A. – volume: 36 start-page: 1018 year: 2009 ident: ref60/cit60 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.11.012 contributor: fullname: Zhang D. – volume: 377 start-page: 162 year: 2008 ident: ref22/cit22 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.12.029 contributor: fullname: Zhang D. – volume: 160 start-page: 65 year: 2003 ident: ref37/cit37 publication-title: J. Magn. Reson. doi: 10.1016/S1090-7807(02)00014-9 contributor: fullname: Schwieters C. D. – volume: 239 start-page: 129 year: 1988 ident: ref38/cit38 publication-title: FEBS Lett. doi: 10.1016/0014-5793(88)80559-3 contributor: fullname: Nilges M. – volume: 131 start-page: 373 year: 1998 ident: ref28/cit28 publication-title: J. Magn. Reson. doi: 10.1006/jmre.1998.1361 contributor: fullname: Ottiger M. – volume: 458 start-page: 445 year: 2009 ident: ref61/cit61 publication-title: Nature doi: 10.1038/nature07961 contributor: fullname: Raiborg C. |
SSID | ssj0004074 |
Score | 2.214016 |
Snippet | Ubiquitin (Ub) modifications are transduced by receptor proteins that use Ub-binding domains (UBDs) to recognize distinct interaction faces on the Ub surface.... |
SourceID | proquest crossref pubmed acs |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 9076 |
SubjectTerms | Amino Acid Motifs - genetics Animals Aspartic Acid - metabolism Cell Line, Tumor Crystallography, X-Ray DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Hydrophobic and Hydrophilic Interactions Models, Molecular Muscle Proteins - chemistry Muscle Proteins - genetics Muscle Proteins - metabolism Mutagenesis, Site-Directed Protein Binding - genetics Protein Structure, Tertiary - genetics Rats Signal Transduction - genetics Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Zinc Fingers - genetics |
Title | Independent Interactions of Ubiquitin-Binding Domains in a Ubiquitin-Mediated Ternary Complex |
URI | http://dx.doi.org/10.1021/bi201137e https://www.ncbi.nlm.nih.gov/pubmed/21923101 https://search.proquest.com/docview/900624729 |
Volume | 50 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwhV1bT8IwFD5BfNAXL-AFL6RR49twdFu3PSJI0ARfhIQXs7RdlyzKUBiJ-Ottuw0x3t6WdN2anm7nO5fvHIALyinx7cgzrDD0DZvIK8aFaxDP55gRjrnmwvTvSW9o342cUQnOf4ng4-YVi5WOslyxButYZQ4q_NN--CQ_mnmpZWkaY4nHi_JBq1OV6uGzr6rnFzyp9Up3GzoFOydLJ3lqzFPW4O_fizX-teQd2MpxJWplB2EXSiKpQLWVSJt6vECXSGd6ahd6BTbaRZe3KjzeLvvgpki7BzOmwwxNIjRk8es8TuPEuI41-wV1JmMay8E4QXRluK8bfogQDZR7cbpA6jfzLN72YNi9GbR7Rt5ywaCWZ6ZGSJuEWsT2fDPkLiVmxDTdyXGoxH4ml2hKKD-ULVwWuowyETm-F0bUY5h7LrP2oZxMEnEIiGMnIiElliqgT6RVwxxHE29Vu2PM7BrUpUyC_JOZBToajpvBcvNqcFaIK3jJSm_8dBMqBBnInVPRDpqIyXwW-IoeKt_k1-AgE_DyKTiDtc2j_5ZwDJs4z_nDzgmU0-lcnEoQkrK6PoQfxwfUPQ |
link.rule.ids | 315,786,790,2782,27109,27957,27958,57093,57143 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1bT4MwFD7x8jBfvM3LvMzGGN9QVmiBR50uU7e9uCV7MaQtJSEqU2GJ-uttC9vUaPSNpFBO2sL5zmm_7wAcMcFo4Ma-5URRYLlUXXEhPYv6gcCcCiwMF6bbo-2Bez0kw1ImR3NhlBGZ6ikzm_gzdYHGKU-0q3I8OQ-LxFNxuIZBzdsZB9IuFZdVhIwVLJ-oCH1-VHsgkX31QL_ASuNeWitFnSJjmDlVcn8yzvmJeP-m2fg_y1dhuUSZ6KxYFmswJ9N1qJ6lKsJ-fEPHyJz7NAn1dag0JzXfqnB3Na2KmyOTLCx4DxkaxWjAk-dxkiepdZ4YLgy6GD2yRDUmKWKfmrum_IeMUF8nG1_ekP7pPMjXDRi0LvvNtlUWYLCY49u5FbEGZQ51_cCOhMeoHXNDfiKEKSRoC4WtpM5KudLjkccZlzEJ_ChmPsfC97izCQvpKJXbgAQmMY0YdbScPlUxDifE0HB18WPM3RrU1diF5QeUhWZvHDfC6eDV4HAya-FTIcTx001oMp-hGjm998FSORpnYaDJoupNQQ22inme9oILkNvY-cuEA6i0-91O2Lnq3ezCEi5PA2KyBwv5y1juK3iS87pZlx84s9yo |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1ZS8QwEB50BfXF-1jPIOJbtZs2afuoq4u3gi74IiVXoeh21XbB9debpN31QNG3Qpp0mCSdbyb5ZgC2mWA08pPQ8aSMHJ_qJy5U4NAwEphTgYXlwlxc0uO2f3pH7ipH0XBhtBC5Him3h_hmVz_JpMow0NjjqTFXXqBGYYyYwt0GCjVvPniQbpV1WXvJWEPzQSahz12NFRL5Vyv0C7S0JqY1DVdD4ezNkofdXsF3xdu3vI3_l34Gpiq0ifbL5TELIyqbg_n9THvanT7aQfb-pw2sz8FEc1D7bR7uT4bVcQtkg4Yl_yFH3QS1efrcS4s0cw5Sy4lBh90OS3VjmiH2qfnClgFREt2aoONLH5mfz6N6XYB26-i2eexUhRgc5oVu4UjWoMyjfhi5UgSMugm3JChCmEaErtAYS5nolK8CLgPOuEpIFMqEhRyLMODeItSybqaWAQlMEioZ9Uxafap9HU6IpeOaIsiY-3XY0PqLq42Ux_aMHDfiofLqsDWYufipTMjx00toMKex1pw5A2GZ6vbyODKkUf2lqA5L5VwPR8El2G2s_CXCJoxfH7bi85PLs1WYxNWlQEzWoFa89NS6RikF37BL8x18Vd8i |
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=Independent+interactions+of+ubiquitin-binding+domains+in+a+ubiquitin-mediated+ternary+complex&rft.jtitle=Biochemistry+%28Easton%29&rft.au=Garner%2C+Thomas+P&rft.au=Strachan%2C+Joanna&rft.au=Shedden%2C+Elizabeth+C&rft.au=Long%2C+Jed+E&rft.date=2011-10-25&rft.eissn=1520-4995&rft.volume=50&rft.issue=42&rft.spage=9076&rft_id=info:doi/10.1021%2Fbi201137e&rft_id=info%3Apmid%2F21923101&rft.externalDocID=21923101 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-2960&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-2960&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-2960&client=summon |