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J Mol Biol. 2009 Sep 25;392(3):787-802. doi: 10.1016/j.jmb.2009.07.057. Epub 2009 Jul 23.

Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.

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Research Department of Shriners Hospital for Children, Portland, OR 97239, USA.


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.

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