Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2
Sun J, Lu S, Ouyang M, Lin L, Zhuo Y, Liu B, Chien S, Neel B, Wang Y. Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2. Nature Communications 2013, 4: 2037. PMID: 23792876, PMCID: PMC3777412, DOI: 10.1038/ncomms3037.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesEmbryo, MammalianExtracellular Signal-Regulated MAP KinasesFibroblastsFluorescence Resonance Energy TransferGenes, ReporterGRB2 Adaptor ProteinHEK293 CellsHumansKineticsMiceMolecular Sequence DataMutant ProteinsMutationPeptidesPhosphorylationPhosphotyrosineProtein BindingProtein ConformationProtein Tyrosine Phosphatase, Non-Receptor Type 11ConceptsCis-interactionsSH2 domainC-terminal phosphotyrosinesProtein tyrosine phosphatase SHP2Amino acid sequenceTyrosine phosphatase SHP2Adaptor proteinModular domainsModular proteinsTrans-regulationAcid sequenceProtein functionPhosphatase SHP2Evolutionary dynamicsBinding site affinityPhosphotyrosineConformational dynamicsProteinGrb2SH2SequenceSHP2Site affinityAntagonist combinationDominant form