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Details on Person Collagen VII triple-helices form an anti-parallel dimer, ass...

Class:IdSummation:2214317
_displayNameCollagen VII triple-helices form an anti-parallel dimer, ass...
_timestamp2012-04-30 16:02:40
created[InstanceEdit:2214325] Jupe, S, 2012-04-30
literatureReference[LiteratureReference:1643671] The tissue form of type VII collagen is an antiparallel dimer
[LiteratureReference:2214326] The carboxyl terminus of type VII collagen mediates antiparallel dimer formation and constitutes a new antigenic epitope for epidermolysis Bullosa acquisita autoantibodies
[LiteratureReference:1643684] Large complex globular domains of type VII procollagen contribute to the structure of anchoring fibrils
[LiteratureReference:2210345] Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen
textCollagen 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).
(summation)[Reaction:2214324] Collagen type VII dimerization [Homo sapiens]
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