1ck4
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(New page: 200px<br /><applet load="1ck4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ck4, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 10:24, 20 November 2007
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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
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