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, B├Ąchinger HP
J Mol Biol. 2009 392 (3): 787-802

PMID: 19631658 · PMCID: PMC3048824 · DOI:10.1016/j.jmb.2009.07.057

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.

MeSH Terms (14)

Amino Acid Sequence Animals Collagen Type XVIII Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Fusion Proteins Sequence Alignment Sequence Homology, Amino Acid

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