1ck4: Difference between revisions

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[[Image:1ck4.gif|left|200px]]
{{Seed}}
[[Image:1ck4.png|left|200px]]


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{{STRUCTURE_1ck4|  PDB=1ck4  |  SCENE=  }}  
{{STRUCTURE_1ck4|  PDB=1ck4  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.'''
===CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10386626}}


==About this Structure==
==About this Structure==
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[[Category: I-domain]]
[[Category: I-domain]]
[[Category: Metal binding]]
[[Category: Metal binding]]
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