Intramolecular autoinhibition of checkpoint kinase 1 is mediated by conserved basic motifs of the C-terminal kinase–associated 1 domain
Emptage RP, Schoenberger MJ, Ferguson KM, Marmorstein R. Intramolecular autoinhibition of checkpoint kinase 1 is mediated by conserved basic motifs of the C-terminal kinase–associated 1 domain. Journal Of Biological Chemistry 2017, 292: 19024-19033. PMID: 28972186, PMCID: PMC5704483, DOI: 10.1074/jbc.m117.811265.Peer-Reviewed Original ResearchConceptsKA1 domainIntramolecular autoinhibitionSer/Thr proteinKinase 1N-terminal kinase domainChk1 kinase activityKey regulatory mechanismTerminal regulatory regionDNA damage repairSite-directed mutagenesisCheckpoint kinase 1Thr proteinChk1 kinaseHuman Chk1Truncation mutantsKinase domainRegulatory regionsKinase activityBasic residuesDamage repairRegulatory mechanismsStructural homologyResidue linkerCell cyclePrimary structureDimerization of Tie2 mediated by its membrane-proximal FNIII domains
Moore JO, Lemmon MA, Ferguson KM. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 4382-4387. PMID: 28396397, PMCID: PMC5410832, DOI: 10.1073/pnas.1617800114.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneHEK293 CellsHumansMiceModels, MolecularMutationNIH 3T3 CellsProtein ConformationProtein DomainsReceptor, TIE-2X-Ray DiffractionConceptsExtracellular regionFNIII domainsResolution X-ray crystal structureMembrane-proximal fibronectin type III domainsDomain-mediated interactionsDifferent cellular contextsLigand-binding regionHigher-order oligomersTie2 activationFibronectin type III domainReceptor tyrosine kinasesTyrosine kinase familyEGF-homology domainThird FNIII domainType III domainPrevious structural studiesStructural studiesHomology domainCellular contextKinase familyDimer interfaceDimerization modeReceptor dimerizationTyrosine kinasePrimary activator