2025
The C2 domain augments Ras GTPase-activating protein catalytic activity
Paul M, Chen D, Vish K, Lartey N, Hughes E, Freeman Z, Saunders T, Stiegler A, King P, Boggon T. The C2 domain augments Ras GTPase-activating protein catalytic activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2418433122. PMID: 39899710, PMCID: PMC11831179, DOI: 10.1073/pnas.2418433122.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinC2 domainActivity of GTPase-activating proteinGTPase-activating protein domainProtein catalytic activityDomain in vitroAllosteric lobeRas GTPasesSequence conservationGTPase activityAlphaFold modelsRasGAPSignaling defectsRasMutationsCatalytic activityConstitutive disruptionCatalytic advantageGTPaseAlphaFoldDomainGenesSynGAPProteinSequence
2022
Molecular basis for integrin adhesion receptor binding to p21-activated kinase 4 (PAK4)
Ha B, Yigit S, Natarajan N, Morse E, Calderwood D, Boggon T. Molecular basis for integrin adhesion receptor binding to p21-activated kinase 4 (PAK4). Communications Biology 2022, 5: 1257. PMID: 36385162, PMCID: PMC9669019, DOI: 10.1038/s42003-022-04157-3.Peer-Reviewed Original ResearchConceptsP21-activated kinase 4Integrin adhesion receptorsMolecular basisAdhesion receptorsIntegrin β5Potential cellular rolesIntegrin β tailsKinase 4Membrane-proximal halfSubstrate-binding grooveSubstrate-binding siteSite-directed mutagenesisCellular rolesPhosphoacceptor sitesΒ tailExtracellular ligandsCytoplasmic signalingCytoplasmic tailKinase domainMultiple kinasesIntegrin complexΒ5 integrinsΒ5TailMutagenesis
2001
G-Protein Signaling Through Tubby Proteins
Santagata S, Boggon T, Baird C, Gomez C, Zhao J, Shan W, Myszka D, Shapiro L. G-Protein Signaling Through Tubby Proteins. Science 2001, 292: 2041-2050. PMID: 11375483, DOI: 10.1126/science.1061233.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCell MembraneCell NucleusCells, CulturedCrystallography, X-RayGene Expression RegulationGTP-Binding Protein alpha Subunits, Gq-G11Heterotrimeric GTP-Binding ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane LipidsMiceModels, BiologicalMolecular Sequence DataNuclear Localization SignalsObesityPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhospholipase C betaPhosphorylationProtein Structure, TertiaryProteinsReceptor, Serotonin, 5-HT2CReceptors, MuscarinicReceptors, SerotoninRecombinant Fusion ProteinsSignal TransductionTranscription FactorsType C PhospholipasesConceptsTubby-like protein 3G protein signalingTubby proteinTubby domainTranscription regulatorsPlasma membranePhospholipase C-betaReceptor-mediated activationHeterotrimeric GTPSignal transductionGene expressionMolecular mechanismsTubbyC betaCarboxyl terminalCell nucleiMaturity-onset obesityProteinX-ray crystallographyProtein 3SignalingRegulatorMembranePhosphatidylinositolTransduction
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 rangeBound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 Ă… resolution
Dong J, Boggon T, Chayen N, Raftery J, Bi R, Helliwell J. Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 Ă… resolution. Acta Crystallographica Section D, Structural Biology 1999, 55: 745-52. PMID: 10089304, DOI: 10.1107/s0907444998016047.Peer-Reviewed Original ResearchConceptsHen egg white lysozymeX-ray dataAdvanced Protein Crystallization FacilityDifferent crystallization methodsLysozyme crystalsCrystal growth environmentProtein structureHen egg-white lysozyme crystalsEgg white lysozymeCrystallization methodProtein crystalsGelĂ… resolutionCrystalsMicrogravity Spacelab (LMS) missionCrystallizationCrystallization FacilityAgarose gelStructureDiffusion methodPhase boundaryPhysics statesOilNumber of methodsLysozyme
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