[HTML][HTML] Single amino acid substitutions in procollagen VII affect early stages of assembly of anchoring fibrils
R Brittingham, M Colombo, H Ito, A Steplewski… - Journal of Biological …, 2005 - ASBMB
Procollagen VII is a homotrimer of 350-kDa pro-α1 (VII) chains, each consisting of a central
collagenous domain flanked by the noncollagenous N-terminal NC1 domain and the C-
terminal NC2 domain. After secretion from cells, procollagen VII molecules form anti-parallel
dimers with a C-terminal 60-nm overlap. Characteristic alignment of procollagen VII
monomers forming a dimer depends on site-specific binding between the NC2 domain and
the triple-helical region adjacent to Cys-2634 of the interacting procollagen VII molecules …
collagenous domain flanked by the noncollagenous N-terminal NC1 domain and the C-
terminal NC2 domain. After secretion from cells, procollagen VII molecules form anti-parallel
dimers with a C-terminal 60-nm overlap. Characteristic alignment of procollagen VII
monomers forming a dimer depends on site-specific binding between the NC2 domain and
the triple-helical region adjacent to Cys-2634 of the interacting procollagen VII molecules …