2007
Ligand-Induced Structural Transitions in ErbB Receptor Extracellular Domains
Dawson JP, Bu Z, Lemmon MA. Ligand-Induced Structural Transitions in ErbB Receptor Extracellular Domains. Structure 2007, 15: 942-954. PMID: 17697999, DOI: 10.1016/j.str.2007.06.013.Peer-Reviewed Original ResearchConceptsExtracellular regionDimerization siteLow-resolution molecular envelopeEpidermal growth factor receptor (EGFR) activationGrowth factor receptor activationAutoinhibitory intramolecular interactionMajor domain rearrangementsSmall-angle X-ray scatteringReceptor extracellular domainDomain rearrangementsEGF receptorExtracellular domainLigand bindingEGFR mutantsReceptor conformationMutantsMolecular envelopeExtended conformationNew insightsReceptor activationCrystallographic studiesConformationIntramolecular interactionsReceptorsX-ray scattering
1997
Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*
Lemmon M, Pinchasi D, Zhou M, Lax I, Schlessinger J. Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*. Journal Of Biological Chemistry 1997, 272: 6311-6317. PMID: 9045650, DOI: 10.1074/jbc.272.10.6311.Peer-Reviewed Original ResearchConceptsStem cell factorKIT dimerizationReceptor dimerizationExtracellular domainCell factorFourth Ig-like domainColony-stimulating factor-1Receptor tyrosine kinasesIg-like domainsCytokine stem cell factorDomain bindsPlatelet-derived growth factorGrowth factorLike domainDimer bindsMost growth factorsTyrosine kinaseDimerization siteConformational changesReceptor KITAnalytical ultracentrifugationForms of KITBivalent bindingFactor 1Dimerization