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Article: Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutions

TitleChanges in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutions
Authors
Issue Date1989
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1989, v. 261 n. 1, p. 253-257 How to Cite?
AbstractThe effect of glycine-to-arginine mutations in the α1(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 fuctional sequelae result from a kinetic defect in collagen helix formation resulting from the mutation.
Persistent Identifierhttp://hdl.handle.net/10722/147338
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBaker, ATen_US
dc.contributor.authorRamshaw, RAMen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.contributor.authorBateman, JFen_US
dc.date.accessioned2012-05-29T06:03:01Z-
dc.date.available2012-05-29T06:03:01Z-
dc.date.issued1989en_US
dc.identifier.citationBiochemical Journal, 1989, v. 261 n. 1, p. 253-257en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147338-
dc.description.abstractThe effect of glycine-to-arginine mutations in the α1(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 fuctional sequelae result from a kinetic defect in collagen helix formation resulting from the mutation.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshArginineen_US
dc.subject.meshCollagen - Geneticsen_US
dc.subject.meshDrug Stabilityen_US
dc.subject.meshGlycineen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMutationen_US
dc.subject.meshOsteogenesis Imperfecta - Genetics - Metabolismen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Denaturationen_US
dc.titleChanges in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutionsen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid2775212-
dc.identifier.scopuseid_2-s2.0-0024391193en_US
dc.identifier.volume261en_US
dc.identifier.issue1en_US
dc.identifier.spage253en_US
dc.identifier.epage257en_US
dc.identifier.isiWOS:A1989AE78400037-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridBaker, AT=7403520313en_US
dc.identifier.scopusauthoridRamshaw, RAM=7004300244en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US

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