PMID: 2116413Aug 15, 1990Paper

Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.

The Journal of Biological Chemistry
A WesterhausenD J Prockop

Abstract

Cultured skin fibroblasts from two probands with lethal variants of osteogenesis imperfecta synthesized type I procollagen that was posttranslationally over-modified. Analysis of cDNAs and genomic DNAs from the two probands demonstrated that proband I had a single-base mutation that converted the codon for glycine alpha 1-631 to a codon for serine, and proband II had a single-base mutation that converted the codon for glycine alpha 1-598 to a codon for serine. Although the two serine-for-glycine substitutions were separated by only 35 residues, they had markedly different effects on the thermal unfolding of the collagen triple helix as assayed by brief protease digestion. The type I procollagen from proband I (serine alpha 1-631) had an essentially normal temperature for thermal unfolding. In contrast, type I procollagen from proband II (serine alpha 1-598) was cleaved to readily identifiable intermediate fragments of about 630 residues at 20 degrees C. With procollagens from both probands, collagenase A fragments containing the first 775 amino acids of the alpha chain domains had a lowered temperature for thermal unfolding as assayed by brief protease digestion. The collagenase A fragments from proband I were cleaved to interm...Continue Reading

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