1aox
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We have determined the high resolution crystal structure of the I domain | + | We have determined the high resolution crystal structure of the I domain from the alpha-subunit of the integrin alpha2beta1, a cell surface adhesion receptor for collagen and the human pathogen echovirus-1. The domain, as expected, adopts the dinucleotide-binding fold, and contains a metal ion-dependent adhesion site motif with bound Mg2+ at the top of the beta-sheet. Comparison with the crystal structures of the leukocyte integrin I domains reveals a new helix (the C-helix) protruding from the metal ion-dependent adhesion site face of the domain which creates a groove centered on the magnesium ion. Modeling of a collagen triple helix into the groove suggests that a glutamic acid side chain from collagen can coordinate the metal ion, and that the C-helix insert is a major determinant of binding specificity. The binding site for echovirus-1 maps to a distinct surface of the alpha2-I domain (one edge of the beta-sheet), consistent with data showing that virus and collagen binding occur by different mechanisms. Comparison with the homologous von Willebrand factor A3 domain, which also binds collagen, suggests that the two domains bind collagen in different ways. |
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bergelson, J | + | [[Category: Bergelson, J M.]] |
[[Category: Emsley, J.]] | [[Category: Emsley, J.]] | ||
| - | [[Category: King, S | + | [[Category: King, S L.]] |
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
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[[Category: integrin]] | [[Category: integrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:48 2008'' |
Revision as of 09:47, 21 February 2008
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I DOMAIN FROM INTEGRIN ALPHA2-BETA1
Contents |
Overview
We have determined the high resolution crystal structure of the I domain from the alpha-subunit of the integrin alpha2beta1, a cell surface adhesion receptor for collagen and the human pathogen echovirus-1. The domain, as expected, adopts the dinucleotide-binding fold, and contains a metal ion-dependent adhesion site motif with bound Mg2+ at the top of the beta-sheet. Comparison with the crystal structures of the leukocyte integrin I domains reveals a new helix (the C-helix) protruding from the metal ion-dependent adhesion site face of the domain which creates a groove centered on the magnesium ion. Modeling of a collagen triple helix into the groove suggests that a glutamic acid side chain from collagen can coordinate the metal ion, and that the C-helix insert is a major determinant of binding specificity. The binding site for echovirus-1 maps to a distinct surface of the alpha2-I domain (one edge of the beta-sheet), consistent with data showing that virus and collagen binding occur by different mechanisms. Comparison with the homologous von Willebrand factor A3 domain, which also binds collagen, suggests that the two domains bind collagen in different ways.
Disease
Known diseases associated with this structure: Glycoprotein Ia deficiency (1) OMIM:[192974], Neonatal alloimmune thrombocytopenia OMIM:[192974]
About this Structure
1AOX is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Crystal structure of the I domain from integrin alpha2beta1., Emsley J, King SL, Bergelson JM, Liddington RC, J Biol Chem. 1997 Nov 7;272(45):28512-7. PMID:9353312
Page seeded by OCA on Thu Feb 21 11:46:48 2008
