Structural basis of collagen recognition by integrin alpha2beta1

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Collagen / chemistry
  • Collagen / metabolism*
  • Integrins / chemistry
  • Integrins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Collagen
  • Signal Transduction


  • Integrins
  • Receptors, Collagen
  • Collagen

Associated data

  • PDB/1DZI