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
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