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

2002; Wiley; Volume: 11; Issue: 2 Linguagem: Inglês

10.1110/ps.32602

1469-896X

Rita Berisio, Luigi Vitagliano, L. Mazzarella, Adriana Zagari,

Bone and Dental Protein Studies

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 Å, 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.