The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.

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Article

The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.

The Journal of biological chemistry - 15 Nov 1991

Deak S B, Scholz P M, Amenta P S, Constantinou C D, Levi-Minzi S A, Gonzalez-Lavin L, Mackenzie J W

Abstract excerpt

We report a case of mild osteogenesis imperfecta in a 56-year-old male undergoing aortic valve replacement surgery. The primary defect in this patient was the substitution of arginine for glycine 85 in one of the two chains of alpha 1(I) procollagen. The thermal stability of the type I collagen synthesized by the patient's cultured skin fibroblasts was examined by enzymatic digestion. Digestion of the mutant type...

Topics

Amino Acid Sequence
Arginine
Base Sequence
Blotting, Northern
Cells, Cultured
DNA
Fibroblasts
Glycine
Humans
Macromolecular Substances

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Male

Middle Aged

Molecular Sequence Data

Mutation

Oligodeoxyribonucleotides

Osteogenesis Imperfecta

Peptide Mapping

Polymerase Chain Reaction

Source

Open in PubMed

Identifiers

PMID: 1718984

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1718984-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.PMID 1718984Read ↗

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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.Semantic proximity Read ↗

Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix.Semantic proximity Read ↗

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 imperfectaSemantic proximity Read ↗

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.Semantic proximity Read ↗

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged SiteSemantic proximity Read ↗

Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Semantic proximity Read ↗

Position of single amino acid substitutions in the collagen triple helix determines their effect on structure of collagen fibrils.Semantic proximity Read ↗

Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype.Semantic proximity Read ↗

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.Semantic proximity Read ↗

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