2022
Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP
Stiegler A, Vish K, Boggon T. Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Structure 2022, 30: 1603-1614.e5. PMID: 36417908, PMCID: PMC9722645, DOI: 10.1016/j.str.2022.10.009.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsSH2 domainSH2-SH3Src homology 2 domainDual SH2 domainsPhosphotyrosine residuesSH3 domainRho GTPasesPhosphotyrosine recognitionTarget proteinsSynergistic bindingPhosphotyrosineP120RasGAPConformational flexibilityProteinSelectivity mechanismAffinity measurementsDomainGTPasesClose proximityCassetteCrystal structureResiduesCompact arrangementBinding
1999
Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis
Boggon T, Shan W, Santagata S, Myers S, Shapiro L. Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis. Science 1999, 286: 2119-2125. PMID: 10591637, DOI: 10.1126/science.286.5447.2119.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlternative SplicingAmino Acid SequenceAnimalsCell LineCell NucleusCrystallography, X-RayDNAEye ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProteinsRecombinant ProteinsSequence AlignmentTranscription FactorsTranscriptional ActivationConceptsTubby-like proteinsTubby proteinTranscription factorsBipartite transcription factorDisease phenotypeMulticellular organismsProtein familyBiochemical functionsBiological functionsFunctional analysisStructural cluesCore domainUnique familyProteinGenetic mutationsTubbyPhenotypeRetinal degenerationFamilyMammalsOrganismsVital roleCrystal structureMutationsBroad range