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
New Structural Insights into High Affinity Membrane Binding By Coagulation Factor V/Va
Kumar S, Stayrook S, Huntington J, Camire R, Krishnaswamy S. New Structural Insights into High Affinity Membrane Binding By Coagulation Factor V/Va. Blood 2014, 124: 4216. DOI: 10.1182/blood.v124.21.4216.4216.Peer-Reviewed Original ResearchSmall-angle X-ray scattering envelopeMembrane bindingPS-containing membranesC-domainMembrane binding functionMembrane-bound configurationHigh-affinity membrane bindingX-ray structureC2 domainBinding to membranesFactor VaBinding variantsBinding to PS-containing membranesC1 domainV-formBinding functionSmall-angle X-ray scatteringConformational rearrangementsEnergetic expenditureMembrane affinityStructural insightsAffinity interactionSites of vascular damageConformational changesPublished structures