Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 392, Issue 3, Pages 787-802Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.07.057
Keywords
collagens XVIII and XV; crystal structure; trimerization domain; non-collagenous domain; endostatin
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Funding
- Shriners Hospital for Children
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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.
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