Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding.

ABSTRACT: The replacement of one Gly in the essential repeating tripeptide sequence of the type I collagen triple helix results in the dominant hereditary bone disorder osteogenesis imperfecta. The mechanism leading to pathology likely involves misfolding and autophagy, although it has been hypothesized that some mutations interfere with known collagen interactions. Here, the effect of Gly replacements within and nearby the integrin binding GFPGER sequence was investigated using a recombinant bacterial collagen system. When a six-triplet human type I collagen sequence containing GFPGER was introduced into a bacterial collagen-like protein, this chimeric protein bound to integrin. Constructs with Gly to Ser substitutions within and nearby the inserted human sequence still formed a trypsin-resistant t

SUBMITTER: Yigit S 

PROVIDER: S-EPMC5009287 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature