Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

被引：41

作者：

Boudko, Sergei P. ^{[1
,2
]}

Sasaki, Takako ^{[1
,2
]}

Engel, Juergen ^{[3
]}

Lerch, Thomas F. ^{[2
]}

Nix, Jay ^{[4
]}

Chapman, Michael S. ^{[2
]}

Baechinger, Hans Peter ^{[1
,2
]}

机构：

[1] Shriners Hosp Children, Res Dept, Portland, OR 97239 USA

[2] Oregon Hlth & Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97239 USA

[3] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

[4] Univ Calif Berkeley, Lawrence Berkeley Lab, Mol Biol Consortium, Adv Light Source Beamline 422, Berkeley, CA 94720 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2009年 / 392卷 / 03期

关键词：

collagens XVIII and XV; crystal structure; trimerization domain; non-collagenous domain; endostatin; P22 TAILSPIKE PROTEIN; HELICAL COILED-COIL; OLIGOMERIZATION DOMAIN; TISSUE DISTRIBUTION; BINDING PROTEIN; NC1; DOMAIN; C-TERMINUS; ENDOSTATIN; STABILIZATION; CHAIN;

D O I：

10.1016/j.jmb.2009.07.057

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：

Collagens contain a unique triple-helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization, and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：787 / 802

页数：16

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