Trimerization and triple helix stabilization of the collagen XIX NC2 domain.

Boudko SP, Engel J, B├Ąchinger HP
J Biol Chem. 2008 283 (49): 34345-51

PMID: 18845531 · PMCID: PMC2662240 · DOI:10.1074/jbc.M806352200

The mechanisms of chain selection and assembly of fibril-associated collagens with interrupted triple helices (FACITs) must differ from that of fibrillar collagens, since they lack the characteristic C-propeptide. We analyzed two carboxyl-terminal noncollagenous domains, NC2 and NC1, of collagen XIX as potential trimerization units and found that NC2 forms a stable trimer and substantially stabilizes a collagen triple helix attached to either end. In contrast, the NC1 domain requires formation of an adjacent collagen triple helix to form interchain disulfide bridges. The NC2 domain of collagen XIX and probably of other FACITs is responsible for chain selection and trimerization.

MeSH Terms (16)

Amino Acid Sequence Animals Biophysics Collagen Dimerization Disulfides Fibril-Associated Collagens Fibrillar Collagens Humans Mice Molecular Sequence Data Oxygen Peptides Protein Structure, Tertiary Sequence Homology, Amino Acid Thermodynamics

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