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
2019
Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide
Chehayeb R, Stiegler AL, Boggon TJ. Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide. PLOS ONE 2019, 14: e0226113. PMID: 31891593, PMCID: PMC6938330, DOI: 10.1371/journal.pone.0226113.Peer-Reviewed Original ResearchConceptsN-terminal SH2 domainSH2 domainPhosphotyrosine peptidesNative gel shiftSite-directed mutagenesisGAP proteinsCo-crystal structurePhosphorylated tyrosineRas pathwayUnliganded formApo formCross-talk occursGel shiftP120RasGAPIsothermal titration calorimetryP190RhoGAPCell growthSpecific conformationCell proliferationProteinX-ray crystal structureTitration calorimetryDisease pathogenesisCrystal structureRho