2020
Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases
Sheetz JB, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttilä R, Preuss F, Suresh K, Stayrook SE, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon MA. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Molecular Cell 2020, 79: 390-405.e7. PMID: 32619402, PMCID: PMC7543951, DOI: 10.1016/j.molcel.2020.06.018.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBaculoviridaeBinding SitesCell Adhesion MoleculesCell LineCloning, MolecularCrystallography, X-RayGene ExpressionHumansMiceModels, MolecularPrecursor Cells, B-LymphoidProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Kinase InhibitorsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Eph FamilyRecombinant ProteinsSf9 CellsSmall Molecule LibrariesSpodopteraStructural Homology, ProteinSubstrate SpecificityConceptsInsulin receptor kinasePseudokinase domainReceptor tyrosine kinasesTyrosine kinaseNon-catalytic functionsATP-binding pocketType II inhibitorsDomain plasticityActivation loopReceptor kinaseInactive conformationStructural insightsPseudokinasesATP siteStructural comparisonAromatic residuesKinaseAlternative interactionsApparent lackImportant roleDomainWntMotifROR1Residues
2017
Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase.
Emptage RP, Lemmon MA, Ferguson KM. Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase. Biochemical Journal 2017, 474: 385-398. PMID: 27879374, PMCID: PMC5317272, DOI: 10.1042/bcj20160792.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBinding SitesCloning, MolecularEnzyme AssaysEscherichia coliGene ExpressionHumansKineticsMitogen-Activated Protein Kinase 1Models, MolecularPeptidesPhospholipidsProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRecombinant ProteinsScattering, Small AngleSubstrate SpecificityX-Ray DiffractionConceptsKA1 domainMAP/microtubule affinity-regulating kinasesMicrotubule affinity-regulating kinaseGroup of kinasesIntramolecular autoinhibitory interactionAnionic phospholipid bindingAnionic phospholipidsSite-directed mutagenesisAutoinhibitory interactionsRegulatory modulesAutoinhibitory roleProtein modulesMembrane-bound targetsRelated kinasesBind membranesFamily kinasesKinase domainProtein kinasePhospholipid activationC-terminusRegulatory mechanismsPhospholipid bindingMechanistic basisKinaseAutoinhibitory activity
2006
Determining selectivity of phosphoinositide-binding domains
Narayan K, Lemmon MA. Determining selectivity of phosphoinositide-binding domains. Methods 2006, 39: 122-133. PMID: 16829131, PMCID: PMC3786563, DOI: 10.1016/j.ymeth.2006.05.006.Peer-Reviewed Original Research
2005
Membrane activity of the phospholipase C-δ1 pleckstrin homology (PH) domain
Flesch FM, Yu JW, Lemmon MA, Burger KN. Membrane activity of the phospholipase C-δ1 pleckstrin homology (PH) domain. Biochemical Journal 2005, 389: 435-441. PMID: 15755258, PMCID: PMC1175121, DOI: 10.1042/bj20041721.Peer-Reviewed Original Research
2000
Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains
Ferguson K, Kavran J, Sankaran V, Fournier E, Isakoff S, Skolnik E, Lemmon M. Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains. Molecular Cell 2000, 6: 373-384. PMID: 10983984, DOI: 10.1016/s1097-2765(00)00037-x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesBlood ProteinsCrystallography, X-RayFatty AcidsHydrogen BondingInositol PhosphatesLipoproteinsModels, MolecularMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphatidylinositolsProtein Structure, SecondarySequence AlignmentSequence Homology, Amino AcidSignal TransductionSrc Homology DomainsSubstrate SpecificityConceptsPleckstrin homology domainPH domainHomology domainDifferent PH domainsPhosphoinositide specificityMembrane recruitmentProtein modulesCellular signalingStructural basisHost proteinsSecond messengerMajor PIAmino acidsX-ray crystal structureProteinDomainPhosphoinositideHead groupsSignalingMessengerBindsCrystal structureRecruitment