Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem J. 1989 Jul 1;261(1):253-7.

Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of alpha 1 (I)-chain glycine-to-arginine substitutions.

Author information

  • 1C.S.I.R.O. Division of Biotechnology, Parkville, Vic. Australia.

Abstract

The effect of glycine-to-arginine mutations in the alpha 1 (I)-chain on collagen triple-helix structure in lethal perinatal osteogenesis imperfecta was studied by determination of the helix denaturation temperature and by computerized molecular modelling. Arginine substitutions at glycine residues 391 and 667 resulted in similar small decreases in helix stability. Molecular modelling suggested that the glycine-to-arginine-391 mutant resulted in only a relatively small localized disruption to the helix structure. Thus the glycine-to-arginine substitutions may lead to only a small structural abnormality of the collagen helix, and it is most likely that the over-modification of lysine, poor secretion, increased degradation and other functional sequelae result from a kinetic defect in collagen helix formation resulting from the mutation.

PMID:
2775212
PMCID:
PMC1138808
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk