2020
The GTPase-activating protein p120RasGAP has an evolutionarily conserved “FLVR-unique” SH2 domain
Jaber Chehayeb R, Wang J, Stiegler AL, Boggon TJ. The GTPase-activating protein p120RasGAP has an evolutionarily conserved “FLVR-unique” SH2 domain. Journal Of Biological Chemistry 2020, 295: 10511-10521. PMID: 32540970, PMCID: PMC7397115, DOI: 10.1074/jbc.ra120.013976.Peer-Reviewed Original ResearchConceptsC-terminal SH2 domainSH2 domainFLVR motifSrc homology 2 domainArginine residuesSalt bridgePhosphotyrosine motifsPeptide-bound formsPhosphopeptide bindingUnrecognized diversityDirect salt bridgeIntramolecular salt bridgeIsothermal titration calorimetryPhosphotyrosineP120RasGAPMotifX-ray crystal structureTitration calorimetryAspartic acidTandem substitutionsResiduesBindingDomainGTPaseP190RhoGAP
2018
The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase
Stiegler AL, Boggon TJ. The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase. Structure 2018, 26: 1451-1461.e4. PMID: 30174148, PMCID: PMC6249675, DOI: 10.1016/j.str.2018.07.015.Peer-Reviewed Original ResearchConceptsP190RhoGAP proteinsN-terminal GTPase domainProtein-protein interaction domainsNucleotide exchange factorsCanonical GTPaseGTPase domainKnown proteinsEffector proteinsExchange factorInteraction domainNucleotide bindingMutational analysisCritical regulatorGTP-MgGTPProteinBiochemical analysisImportant groupBindingDomainPseudoenzymesGTPase