Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proα1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfecta

Abstract excerpt

Type I procollagen is a heterotrimer comprised of two proalpha1(I) chains and one proalpha2(I) chain. Chain recognition, association, and alignment of proalpha chains into correct registration are thought to occur through interactions between the C-terminal propeptide domains of the three chains. The C-propeptide of each chain contains a series of cysteine residues (eight in proalpha1(I) and seven in...

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