Trimerization and triple helix stabilization of the collagen XIX NC2 domain.
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.
Research Department, Shriners Hospital for Children, Portland, Oregon 97239, USA.
Sergei P
SP
Boudko
Jürgen
J
Engel
Hans Peter
HP
Bächinger
D000595:Amino Acid Sequence; D000818:Animals; D001703:Biophysics / Q000379:methods; D003094:Collagen / Q000737:chemistry* / Q000502:physiology; D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D024021:Fibril-Associated Collagens; D024022:Fibrillar Collagens / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010100:Oxygen / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
C534489:COL19A1 protein, human; D004220:Disulfides; D024021:Fibril-Associated Collagens; D024022:Fibrillar Collagens; D010455:Peptides; C425332:col19a1 protein, mouse; D003094:Collagen; D010100:Oxygen