1K6F | pdb_00001k6f

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

(2002) Protein Sci 11: 262-270

• PubMed: 11790836 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1110/ps.32602
• Primary Citation of Related Structures:  
  1K6F


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy.