Structural basis of collagen recognition by integrin alpha2beta1.
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.
Emsley
J
J
Department of Biochemistry, University of Leicester, United Kingdom.
Knight
C G
CG
Farndale
R W
RW
Barnes
M J
MJ
Liddington
R C
RC
D000595:Amino Acid Sequence; D001665:Binding Sites; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D016023:Integrins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D038981:Receptors, Collagen; D015398:Signal Transduction
D016023:Integrins; D038981:Receptors, Collagen; D003094:Collagen