Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.

doi:10.1042/bj3110815

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Article

Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.

The Biochemical journal - 1 Nov 1995

Culbert A A, Lowe M P, Atkinson M, Byers P H, Wallis G A, Kadler K E

Abstract excerpt

We identified two infants with lethal (type II) osteogenesis imperfecta (OI) who were heterozygous for mutations in the COL1A1 gene that resulted in substitutions of aspartic acid for glycine at position 220 and arginine for glycine at position 664 in the product of one COL1A1 allele in each individual. In normal age- and site-matched bone, approximately 70% (by number) of the collagen fibrils were encrusted with...

Topics

Adult
Arginine
Aspartic Acid
Bone and Bones
Calcification, Physiologic
Collagen
Cyanogen Bromide
Durapatite
Electrophoresis, Polyacrylamide Gel
Female

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glycine

Heterozygote

Humans

Macromolecular Substances

Mutation

Osteogenesis Imperfecta

Peptide Mapping

Pregnancy

Source

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Identifiers

PMID: 7487936
DOI: 10.1042/bj3110815
PMCID: PMC1136074

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7487936-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.PMID 7487936Read ↗

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