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

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.

SUBMITTER: Boudko SP

PROVIDER: S-EPMC3048824 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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

Boudko Sergei P SP Sasaki Takako T Engel Jürgen J Lerch Thomas F TF Nix Jay J Chapman Michael S MS Bächinger Hans Peter HP

Journal of molecular biology 20090723 3

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 ...[more]

PMID: 19631658

Similar Datasets

Crystal structure of the human collagen XV trimerization domain: a potent trimerizing unit common to multiplexin collagens.

Project description:Correct folding of the collagen triple helix requires a self-association step which selects and binds ?-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four ?-sheets and an ?-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by ?-sheet planes from each monomer. The trimerization domain is extremely stable and forms at picomolar concentrations. It is found that the trimerization domain of type XV collagen is structurally similar to that of type XVIII, despite only 32% sequence identity. High structural conservation indicates that the multiplexin trimerization domain represents a three dimensional fold that allows for sequence variability while retaining structural integrity necessary for tight and efficient trimerization.

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