1ck4

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[[Image:1ck4.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck4 OCA], [http://www.ebi.ac.uk/pdbsum/1ck4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ck4 RCSB]</span>
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'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.'''
'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.'''
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[[Category: Pepinsky, R B.]]
[[Category: Pepinsky, R B.]]
[[Category: Venyaminov, S Y.]]
[[Category: Venyaminov, S Y.]]
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[[Category: adhesion]]
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[[Category: Adhesion]]
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[[Category: collagen]]
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[[Category: Collagen]]
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[[Category: i-domain]]
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[[Category: I-domain]]
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[[Category: metal binding]]
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[[Category: Metal binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:49:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:11 2008''
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Revision as of 09:49, 2 May 2008

Template:STRUCTURE 1ck4

CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.


Overview

The alpha1beta1 integrin is a major cell surface receptor for collagen. Ligand binding is mediated, in part, through a 200 amino acid inserted 'I'-domain contained in the extracellular part of the integrin alpha chain. Integrin I-domains contain a divalent cation binding (MIDAS) site and require cations to interact with integrin ligands. We have determined the crystal structure of recombinant I-domain from the rat alpha1beta1 integrin at 2.2 A resolution in the absence of divalent cations. The alpha1 I-domain adopts the dinucleotide binding fold that is characteristic of all I-domain structures that have been solved to date and has a structure very similar to that of the closely related alpha2beta1 I-domain which also mediates collagen binding. A unique feature of the alpha1 I-domain crystal structure is that the MIDAS site is occupied by an arginine side chain from another I-domain molecule in the crystal, in place of a metal ion. This interaction supports a proposed model for ligand-induced displacement of metal ions. Circular dichroism spectra determined in the presence of Ca2+, Mg2+ and Mn2+ indicate that no changes in the structure of the I-domain occur upon metal ion binding in solution. Metal ion binding induces small changes in UV absorption spectra, indicating a change in the polarity of the MIDAS site environment.

About this Structure

1CK4 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function., Nolte M, Pepinsky RB, Venyaminov SYu, Koteliansky V, Gotwals PJ, Karpusas M, FEBS Lett. 1999 Jun 11;452(3):379-85. PMID:10386626 Page seeded by OCA on Fri May 2 12:49:17 2008

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