The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence

被引:157
作者
Kramer, RZ
Bella, J
Brodsky, B
Berman, HM
机构
[1] Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA
[2] Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08855 USA
[3] Rutgers State Univ, Waksman Inst, Piscataway, NJ 08855 USA
关键词
collagen; triple helix; hydroxyproline; hydration; intermolecular assembly;
D O I
10.1006/jmbi.2001.4849
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
A detailed description of the 2.0 Angstrom structure of the triple-helical peptide, (Pro-Hyp-Gly)(3)-Ile-Thr-Gly-Ala-Arg-Gly-Leu-Ala-Gly-Pro-Hyp-Gly-(Pro-Hyp-Gly)(3), denoted as T3-785, is presented. This peptide contains a biologically relevant sequence and was designed to model the imino acid-poor 785-796 region of human type III collagen just C-terminal to the matrix metalloproteinase cleavage site. The crystal structure of the T3-785 peptide demonstrates that sequence can influence local conformational changes in triple-helical structure, in terms of superhelical pitch, hydrogen bonding pattern, and hydration patterns. The novel packing arrangement displayed by the T3-785 structure, compared with those of collagen-like peptides with more imino acid-rich sequences indicates the sequence dependence of intermolecular assemblies in collagen as well. The observed synergy between the packing arrangements and the extended hydration network indicates that hydration of the triple helix is directly related to its association with other molecules. (C) 2001 Academic Press.
引用
收藏
页码:131 / 147
页数:17
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