Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

Sergei P. Boudko, Takako Sasaki, Jürgen Engel, Thomas F. Lerch, Jay Nix, Michael S. Chapman, Hans Peter Bächinger

Research output: Contribution to journalArticle

24 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)787-802
Number of pages16
JournalJournal of molecular biology
Volume392
Issue number3
DOIs
StatePublished - Sep 25 2009

Keywords

  • collagens XVIII and XV
  • crystal structure
  • endostatin
  • non-collagenous domain
  • trimerization domain

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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