1997
Two EGF molecules contribute additively to stabilization of the EGFR dimer
Lemmon M, Bu Z, Ladbury J, Zhou M, Pinchasi D, Lax I, Engelman D, Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. The EMBO Journal 1997, 16: 281-294. PMID: 9029149, PMCID: PMC1169635, DOI: 10.1093/emboj/16.2.281.Peer-Reviewed Original ResearchConceptsEpidermal growth factorReceptor dimerizationEGF moleculesPrecise molecular detailsHuman growth hormone receptorReceptor-receptor interactionsGrowth factorInterferon-gamma receptorEGFR dimersSignaling eventsMolecular detailsReceptor oligomerizationGrowth hormone receptorExtracellular domainEGFR familyCell surfaceMonomer bindsSubsequent associationDimerizationHormone receptorsTitration calorimetrySmall-angle X-ray scatteringBindingReceptorsMultivalent binding
1979
Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.
Pickover C, McKay D, Engelman D, Steitz T. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. Journal Of Biological Chemistry 1979, 254: 11323-11329. PMID: 387770, DOI: 10.1016/s0021-9258(19)86488-8.Peer-Reviewed Original ResearchConceptsYeast phosphoglycerate kinasePhosphoglycerate kinaseConformational changesTernary complexSubstrate bindingHinge motionKinaseSubstrate MgATPCleft closureSmall-angle X-raySeparate bindingRadius of gyrationAngle X-rayMgATPBindingApparent similarityComplexesCleftEnzymeObserved changesHexokinaseGyration decreasesDomainSimilarity