Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion.

Abstract excerpt

Dermal fibroblasts from a fetus with perinatal lethal OI synthesized normal and abnormal type I procollagen molecules. The abnormal molecules contained one or two pro alpha 1 (I) chains in which glycine at position 847 in the triple helical region was substituted by arginine as the result of a de novo G-to-A transition in the first base of the glycine codon. The substitution resulted in increased...

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