Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10

被引：55

作者：

Nagarajan, V ^{[1
]}

Kamitori, S ^{[1
]}

Okuyama, K ^{[1
]}

机构：

[1] Tokyo Univ Agr & Technol, Fac Technol, Dept Biotechnol & Life Sci, Koganei, Tokyo 1848588, Japan

来源：

JOURNAL OF BIOCHEMISTRY | 1998年 / 124卷 / 06期

关键词：

collagen; hydration; hydroxyproline; model peptide; triple helix;

D O I：

10.1093/oxfordjournals.jbchem.a022229

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Single crystals of (Pro-Pro-Gly)(10) were grown by the hanging drop method, The crystals diffracted to a resolution of 1.8 Angstrom. In the crystals the polypeptides form triple helices that aggregate end-to-end mediated by the solvent molecules, with the basic repeat being 20 Angstrom along the helical axis. Analysis of the 20 Angstrom structure of (Pro-Pro-Gly)(10) using data up to a resolution of 1.9 Angstrom revealed that the overall structure is in accordance with the 7/2 model proposed for collagen, The three strands are held together by the (Gly) N-H ... O (Pro-X) hydrogen bond interactions, and additional stability is provided by the (Pro-Y) C-alpha-H ... O (Pro-X) hydrogen bonding interactions.

引用

页码：1117 / 1123

页数：7

共 27 条

[1] HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE [J].