2016
Structural Basis for the Procofactor to Cofactor Transition in Human Factor V
Kumar S, Deng W, Stayrook S, Li R, Camire R, Krishnaswamy S. Structural Basis for the Procofactor to Cofactor Transition in Human Factor V. Blood 2016, 128: 253. DOI: 10.1182/blood.v128.22.253.253.Peer-Reviewed Original ResearchBasic regionB domainC-terminusLong standing puzzleBR bindingCrystal structureDocking studiesBr fragmentsHuman factor VCentral B domainA2 domainAmide proton exchange ratesPhosphatidylserine-containing membranesAr2Hydrogen-deuterium exchangeA1-A2-B-A3-C1-C2Adjacent regionsAmide proton exchangeComputational docking studiesProton exchange ratesDomain organizationAcid sequenceProteolytic excisionCofactor formationPrimary structure
2008
Substrate Discrimination among Mitogen-activated Protein Kinases through Distinct Docking Sequence Motifs*
Sheridan DL, Kong Y, Parker SA, Dalby KN, Turk BE. Substrate Discrimination among Mitogen-activated Protein Kinases through Distinct Docking Sequence Motifs*. Journal Of Biological Chemistry 2008, 283: 19511-19520. PMID: 18482985, PMCID: PMC2443660, DOI: 10.1074/jbc.m801074200.Peer-Reviewed Original ResearchConceptsDEF sitesProtein kinaseMAPK isoformsSequence requirementsMAPK signal transduction cascadePhosphorylation site motifsMAPK family membersSignal transduction cascadePeptide library screenDocking motifExtracellular stimuliMAPK interactionPhosphorylation sitesSequence motifsTransduction cascadeSite motifSubstrate specificityKey residuesSequence specificityLibrary screenUnique sequencesIndividual MAPKsCellular responsesComputational docking studiesExquisite specificity
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