Effects of Mutations that Change Primary Structure of Collagen on the Self-Assembly of the Protein into Fibrils
We have recently observed that a single base mutation in a gene for type I procollagen converts a glycine residue to cysteine and that the substitution for the glycyl residue has a remarkable effect both on the conformation of the molecule and the morphology of the fibrils that are formed as the mutated procollagen molecule is processed to collagen (Vogel et al., 1987; 1988; Kadler et al., 1988b). The observations have largely been made possible through the development of a new system for examining the self-assembly of collagen de novo (Kadler et al., 1987; 1988a).
KeywordsCollagen Fibril Osteogenesis Imperfecta Triple Helix Cysteine Mutation Collagen Triple Helix
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