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Collagen type VII dimerization
Stable Identifier
R-HSA-2214324
Type
Reaction [binding]
Species
Homo sapiens
Compartment
extracellular region
ReviewStatus
5/5
Locations in the PathwayBrowser
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Extracellular matrix organization (Homo sapiens)
Collagen formation (Homo sapiens)
Assembly of collagen fibrils and other multimeric structures (Homo sapiens)
Anchoring fibril formation (Homo sapiens)
Collagen type VII dimerization (Homo sapiens)
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The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Collagen VII triple-helices form an anti-parallel dimer, associating through disulfide bonds formed in a 60-nm overlap (NC2 domain) of the amino terminal triple helical ends. A portion of this region is proteolytically removed (Morris et al. 1986, Chen et al. 2001) prior to aggregation of dimers into anchoring fibrils (Lundstrum et al. 1986).
Literature References
PubMed ID
Title
Journal
Year
3082888
The tissue form of type VII collagen is an antiparallel dimer
Bentz, H
,
Keene, DR
,
Burgeson, RE
,
Glanville, RW
,
Morris, NP
J Biol Chem
1986
Participants
Input
x 2
Collagen alpha-1(VII) trimer [extracellular region]
(Homo sapiens)
Output
Collagen type VII hexamer [extracellular region]
(Homo sapiens)
Participates
as an event of
Anchoring fibril formation (Homo sapiens)
Orthologous Events
Collagen type VII dimerization (Caenorhabditis elegans)
Collagen type VII dimerization (Mus musculus)
Collagen type VII dimerization (Rattus norvegicus)
Collagen type VII dimerization (Sus scrofa)
Collagen type VII dimerization (Xenopus tropicalis)
Authored
Jupe, S (2012-04-30)
Reviewed
Raleigh, S (2012-10-08)
Ricard-Blum, S (2012-11-19)
Kalamajski, S (2012-10-08)
Created
Jupe, S (2012-04-30)
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