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

ABSTRACT: 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.

SUBMITTER: Boudko SP

PROVIDER: S-EPMC2662240 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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

Boudko Sergei P SP Engel Jürgen J Bächinger Hans Peter HP

The Journal of biological chemistry 20081008 49

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 o ...[more]

PMID: 18845531

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