1aox

File:1aox.gif

spinqualitylabelsall models 1aox, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

I DOMAIN FROM INTEGRIN ALPHA2-BETA1

OverviewOverview

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.

About this StructureAbout this Structure

1AOX is a Single protein structure of sequence from Homo sapiens with MG as ligand. Structure known Active Sites: MGA and MGB. Full crystallographic information is available from OCA.

ReferenceReference

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

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