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Article

Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders

1 Jan 2004

Abstract excerpt

A missense mutation leading to the replacement of one Gly in the (Gly-Xaa-Yaa)n repeat of the collagen triple helix can cause a range of heritable connective tissue disorders that depend on the gene in which the mutation occurs. Osteogenesis imperfecta results from mutations in type I collagen, Ehlers-Danlos syndrome type IV from mutations in type III collagen, Alport syndrome from mutations in type IV collagen,...

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PMID: 15365990
DOI: 10.1002/humu.20091

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Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disordersPMID 15365990Read ↗

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

Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta.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 ↗

Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.Semantic proximity Read ↗

Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Semantic proximity Read ↗

Local sequence context determines the effect of glycine substitutions in collagen triple helicesSemantic proximity Read ↗

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

Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels.Semantic proximity Read ↗

Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations.Semantic 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 ↗

Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.Semantic proximity Read ↗

Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity.Semantic proximity Read ↗

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