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Cell. 2000 Mar 31;101(1):47-56.

Structural basis of collagen recognition by integrin alpha2beta1.

Author information

1
Department of Biochemistry, University of Leicester, United Kingdom.

Abstract

We have determined the crystal structure of a complex between the I domain of integrin alpha2beta1 and a triple helical collagen peptide containing a critical GFOGER motif. Three loops on the upper surface of the I domain that coordinate a metal ion also engage the collagen, with a collagen glutamate completing the coordination sphere of the metal. Comparison with the unliganded I domain reveals a change in metal coordination linked to a reorganization of the upper surface that together create a complementary surface for binding collagen. Conformational changes propagate from the upper surface to the opposite pole of the domain, suggesting both a basis for affinity regulation and a pathway for signal transduction. The structural features observed here may represent a general mechanism for integrin-ligand recognition.

PMID:
10778855
DOI:
10.1016/S0092-8674(00)80622-4
[Indexed for MEDLINE]
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