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. 2000 Mar 31;101(1):47-56.
doi: 10.1016/S0092-8674(00)80622-4.

Structural basis of collagen recognition by integrin alpha2beta1

J Emsley  1 , C G Knight, R W Farndale, M J Barnes, R C Liddington
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Free article

Structural basis of collagen recognition by integrin alpha2beta1

J Emsley et al. Cell. .
Free article

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.

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