Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)

Protein Sci. 2002 Feb;11(2):262-70. doi: 10.1110/ps.32602.


The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)(10)](3) is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 A, using synchrotron radiation. The final model, which was refined to an R(factor) of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)(10)](3) packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Collagen / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Glycine
  • Hydrogen Bonding
  • Models, Molecular
  • Oligopeptides / chemistry*
  • Peptides / chemistry*
  • Proline
  • Protein Conformation


  • Oligopeptides
  • Peptides
  • prolyl-prolyl-glycine
  • Collagen
  • Proline
  • Glycine

Associated data

  • PDB/1K6F