1k6f
From Proteopedia
Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)., Berisio R, Vitagliano L, Mazzarella L, Zagari A, Protein Sci. 2002 Feb;11(2):262-70. PMID:11790836 Page seeded by OCA on Fri May 2 22:21:44 2008
