Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins
Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggests that they may be concerned with...
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Published in | International journal of biological macromolecules Vol. 11; no. 1; pp. 56 - 58 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.02.1989
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Subjects | |
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Abstract | Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggests that they may be concerned with binding to cell-surface receptors. |
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AbstractList | Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggests that they may be concerned with binding to cell-surface receptors. Beta-lactoglobulin has been found to be a member of a super family of protein that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggest that they may be concerned with binding to cell-surface receptors. |
Author | North, A.C.T. |
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Cites_doi | 10.1016/0022-2836(87)90476-1 10.1016/0022-2836(87)90296-8 10.1042/bst0130265 10.1038/327659a0 10.1126/science.3388043 10.1002/j.1460-2075.1987.tb02401.x 10.1016/0022-2836(87)90661-9 10.1016/0968-0004(88)90031-X 10.1126/science.2580349 10.1038/324383a0 |
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Keywords | ligand binding Beta-lactoglobulin protein homology |
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References | Huber, Schneider, Mayr, Muller, Deutzmann, Suter, Zuber, Falk, Kayser (BIB7) 1987; 198 Sawyer (BIB8) 1987; 327 Pervaiz, Brew (BIB12) 1985; 228 Holden, Rypniewski, Law, Rayment (BIB5) 1987; 6 Godovac-Zimmermann (BIB9) 1988; 13 Pevsner, Reed, Feinstein, Snyder (BIB10) 1988; 241 Jones, Bergfors, Sedzik, Unge (BIB15) 1988; 185 Sivaprasadarao, Findley (BIB14) 1988; 255 Monaco, Zanotti, Spadon, Bolognesi, Sawyer, Eliopoulos (BIB4) 1987; 197 North, A.C.T. Yewdall, S.J. (unpublished work) Yewdall, S. J. (personal communication) Sawyer, Papiz, North, Eliopoulos (BIB1) 1985; 13 Huber, Schneider, Epp, Mayr, Messerschmitt, Pflugrath, Kayser (BIB6) 1987; 195 Papiz, Sawyer, Eliopoulos, North, Findlay, Sivaprasadarao, Jones, Newcomer, Kraulis (BIB2) 1986; 324 Findlay, J.B. C. (personal communication) Sawyer (10.1016/0141-8130(89)90041-X_BIB8) 1987; 327 Huber (10.1016/0141-8130(89)90041-X_BIB6) 1987; 195 Monaco (10.1016/0141-8130(89)90041-X_BIB4) 1987; 197 Jones (10.1016/0141-8130(89)90041-X_BIB15) 1988; 185 10.1016/0141-8130(89)90041-X_BIB13 10.1016/0141-8130(89)90041-X_BIB11 Godovac-Zimmermann (10.1016/0141-8130(89)90041-X_BIB9) 1988; 13 Huber (10.1016/0141-8130(89)90041-X_BIB7) 1987; 198 Pevsner (10.1016/0141-8130(89)90041-X_BIB10) 1988; 241 Holden (10.1016/0141-8130(89)90041-X_BIB5) 1987; 6 Sivaprasadarao (10.1016/0141-8130(89)90041-X_BIB14) 1988; 255 Pervaiz (10.1016/0141-8130(89)90041-X_BIB12) 1985; 228 10.1016/0141-8130(89)90041-X_BIB3 Sawyer (10.1016/0141-8130(89)90041-X_BIB1) 1985; 13 Papiz (10.1016/0141-8130(89)90041-X_BIB2) 1986; 324 |
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Snippet | Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid... Beta-lactoglobulin has been found to be a member of a super family of protein that bind specific ligands and which share common features in their amino acid... |
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SubjectTerms | Amino Acid Sequence Animals Beta-lactoglobulin Carrier Proteins - chemistry Carrier Proteins - metabolism Humans Lactoglobulins - chemistry Lactoglobulins - metabolism ligand binding Ligands Models, Molecular Molecular Sequence Data protein homology Sequence Homology, Nucleic Acid |
Title | Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins |
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