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
2011
High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation
Kumar S, Stayrook S, Huntington J, Camire R, Krishnaswamy S. High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation. Blood 2011, 118: 375. DOI: 10.1182/blood.v118.21.375.375.Peer-Reviewed Original ResearchC2 domainA2 domainVenom proteinsB domainVenom of Pseudonaja textilisMembrane-dependent reactionsA1-A2-B-A3-C1-C2Absence of membranesMammalian coagulationSequence alignmentMammalian blood coagulationDomain organizationMolecular replacementRegulating blood coagulationToxin repertoireProtruding loopBinding to membranesHydrophobic residuesProteolytic processingBind membranesResolution structureMembrane bindingA-resolutionActivation of human prothrombinProteolytic activity