The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer
Mudumbi K, Julius A, Herrmann J, Li E. The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer. The Journal Of Membrane Biology 2013, 246: 487-493. PMID: 23727984, DOI: 10.1007/s00232-013-9563-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SubstitutionBone Diseases, DevelopmentalHumansMutation, MissenseNeoplasmsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryReceptor, Fibroblast Growth Factor, Type 3ConceptsFGFR3 transmembrane domainFibroblast growth factor receptor 3Transmembrane domainA391E mutationSingle-pass membrane proteinCytosolic kinase domainTransmembrane domain dimerReceptor tyrosine kinase familyTyrosine kinase familyGrowth factor receptor 3TMD dimersCytosolic domainKinase familyTransmembrane proteinMembrane proteinsKinase domainDomain dimerExtracellular domainGenetic studiesDistinct domainsActivity assaysStable dimerCranial dysplasiaMutationsMotif