Dimerization of procollagen type VI

Stable Identifier
R-HSA-1614460
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Collagen type VI forms dimers and tetramers before secretion (Furthmayr et al. 1983, von der Mark et al. 1984, Engel et al. 1985, Colombatti et al. 1987). The monomers associate in antiparallel with a 30nm axial shift, intertwining 4 or 5 times (Furthmayr et al. 1983). These associate laterally to form tetramers (Furthmayr et al. 1983, von der Mark et al. 1984)The tetramers associate to form microfibrils in a non-covalent manner, presumed to be mediated through A domain interactions (Baldock et al. 2003). Collagen type VI chains are extensively post translationally modifed by the hydroxylation of proline and lysine residues (Myllyharju & Kivirikko 2004) and subsequent glycosylation of hydroxylysine, thought to be essential for tetramer formation and secretion (Sipila et al. 2007).

Literature References
PubMed ID Title Journal Year
12473679 Structural basis of type VI collagen dimer formation

Ball, S, Bella, J, Shuttleworth, A, Kielty, CM

J Biol Chem 2003
6307276 Electron-microscopical approach to a structural model of intima collagen

Furthmayr, H, Wiedemann, H, Timpl, R, Odermatt, E, Engel, J

Biochem J 1983
3938630 Structure and macromolecular organization of type VI collagen

Engel, J, Furthmayr, H, Odermatt, E, von der Mark, H, Aumailley, M, Fleischmajer, R, Timpl, R

Ann N Y Acad Sci 1985
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