Nagarajan V, Kamitori S, Okuyama K
Department of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, Naka-cho, Koganei, Tokyo, 184-8588, Japan.
J Biochem. 1999 Feb;125(2):310-8. doi: 10.1093/oxfordjournals.jbchem.a022288.
The crystal structure of a triple helical peptide (Pro-Hyp-Gly)10 has been determined at 1.9 A resolution. Single crystals grown by the hanging drop method, diffracted to a resolution of 1.8 A. The polymer-like structure of the triple helical repeat Pro-Hyp-Gly was in accordance with the 7/2 model proposed for collagen and very similar to the previously determined structure with a Pro-Pro-Gly sequence repeat. The solvent structure was also very similar to that previously observed, showing similar hydration patterns, but different crystal packing. The presence of hydroxyproline did not have any effect on the molecular structure or the hydration structure. This is in accordance with the recent finding that the inductive effect of the hydroxyl group attached to the Cgamma atom of hydroxyproline enhances collagen stability rather than the extensive water network.
已在1.9埃分辨率下测定了三螺旋肽（脯氨酸-羟脯氨酸-甘氨酸）10的晶体结构。通过悬滴法生长的单晶衍射分辨率达到1.8埃。三螺旋重复序列脯氨酸-羟脯氨酸-甘氨酸的类聚合物结构与为胶原蛋白提出的7/2模型一致，并且与先前确定的具有脯氨酸-脯氨酸-甘氨酸序列重复的结构非常相似。溶剂结构也与先前观察到的非常相似，显示出相似的水合模式，但晶体堆积不同。羟脯氨酸的存在对分子结构或水合结构没有任何影响。这与最近的发现一致，即连接到羟脯氨酸Cγ原子上的羟基的诱导效应增强了胶原蛋白的稳定性，而不是广泛的水网络。
