[HTML][HTML] Structural basis of collagen recognition by integrin α2β1

J Emsley, CG Knight, RW Farndale, MJ Barnes… - Cell, 2000 - cell.com
J Emsley, CG Knight, RW Farndale, MJ Barnes, RC Liddington
Cell, 2000cell.com
We have determined the crystal structure of a complex between the I domain of integrin
α2β1 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 …
Abstract
We have determined the crystal structure of a complex between the I domain of integrin α2β1 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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