Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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DOI：
10.1110/ps.32602
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发表时间：
2002-02-01
期刊：
影响因子：
8
通讯作者：
Zagari, A
中科院分区：
文献类型：
--
作者：
Berisio, R;Vitagliano, L;Zagari, A
首次报道了胶原样多肽[（Pro-Pro-Gly）（10）]（3）的全长结构。这种结构是从微重力环境中生长的晶体中获得的，使用同步辐射衍射高达1.3埃。最终模型经过优化，R因子为0.18，是迄今为止报道的胶原蛋白三螺旋的最高分辨率描述。该结构提供了关于与胶原蛋白三螺旋结构和组装相关的一系列方面的线索。脯氨酸起皱对Pro-Pro-Gly三联体内部位置的严格依赖性以及主链和侧链二面角之间的相关性支持由羟脯氨酸诱导的三螺旋稳定/不稳定的基于倾向的机制。此外，对[（Pro-Pro-Gly）（10）]（3）堆积的分析（由静电相互作用控制）表明，电荷可能在胶原原纤维中三螺旋的轴向组织中起锁定作用。
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 Angstrom, 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.