2015
The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox
Kumar S, Stayrook S, Camire R, Krishnaswamy S. The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox. Blood 2015, 126: 121. DOI: 10.1182/blood.v126.23.121.121.Peer-Reviewed Original ResearchB domainAcid regionC-terminusCofactor functionBR bindingDiffraction quality crystalsCoagulation factor VA3 domainFactor VaCofactor activityHomologous A domainsA1-A2-B-A3-C1-C2Ca2+-dependent fashionDomain organizationMolecular replacementAcid sequenceXa bindingSingle chain antibodyPrimary sequenceProteolytic excisionDevelopment of novel strategiesBind calcium ionsProteolytic processingProteolytic cleavageStructure-based model
2014
X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase
Kumar S, Sullenger B, Stayrook S, Krishnaswamy S. X-Ray Structure of an Anticoagulant RNA Aptamer Bound to Factor Xa. Structural Basis for Its Ability to Disrupt Interactions Between Xa and Va within Prothrombinase. Blood 2014, 124: 4232. DOI: 10.1182/blood.v124.21.4232.4232.Peer-Reviewed Original ResearchRNA aptamersC-terminusBinding to factor VIIIaIntrinsic XaseBase-paired stemActive site functionAssembly of prothrombinaseFactor Xa and factor VaSELEX screeningMolecular replacementInteracting proteinsProteinase domainFunctional characterizationAptamer bindingCatalytic Ser195Disrupt interactionsA-resolutionFactor XaHeparin bindingStructural basisAutolysis loopNucleotideInteracting speciesNucleotide basesSolvent accessible surface area
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