1K6F

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

1K6F の概要

• エントリーDOI: 10.2210/pdb1k6f/pdb
• 分子名称: collagen triple helix (2 entities in total)
• 機能のキーワード: collagen stability, puckering, amino acid preferences, triple helix, structural protein
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 15184.97

構造登録者

Berisio, R.,Vitagliano, L.,Mazzarella, L.,Zagari, A. (登録日: 2001-10-16, 公開日: 2002-01-30, 最終更新日: 2024-02-07)

主引用文献

Berisio, R.,Vitagliano, L.,Mazzarella, L.,Zagari, A.
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)
Protein Sci., 11:262-270, 2002

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.

PubMed: 11790836
DOI: 10.1110/ps.32602

実験手法

X-RAY DIFFRACTION (1.3 Å)