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    J Mol Biol. 2009 Sep 25;392(3):787-802. Epub 2009 Jul 23.

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

    Boudko SP, Sasaki T, Engel J, Lerch TF, Nix J, Chapman MS, Bächinger HP.

    Source

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

    Abstract

    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.

    PMID:
    19631658
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3048824
    Free PMC Article

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