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http://purl.uniprot.org/citations/11148028http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11148028http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11148028http://www.w3.org/2000/01/rdf-schema#comment"The binding of von Willebrand factor (vWF) to the platelet receptor, glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of thrombus formation and is regulated by interactions with extracellular matrix components under the influence of hemodynamic forces. To a certain extent, these effects can be mimicked in vitro by two nonphysiologic modulators, ristocetin and botrocetin. The latter, isolated from the venom of the snake Bothrops jararaca, is a 31-kDa heterodimeric protein that forms a soluble complex with vWF. As an initial step toward understanding the mechanisms that regulate vWF function, we have solved the crystal structure of botrocetin at 1.8 A resolution. Botrocetin exhibits homology with other snake proteins, but contains only one metal binding site as compared to two in Factor IX binding protein and Factor IX/X binding protein and none in flavocetin. A distinctive feature of botrocetin is the presence of a negatively charged surface that may play a role in the association with the vWF A1 domain."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.org/dc/terms/identifier"doi:10.1021/bi0021737"xsd:string
http://purl.uniprot.org/citations/11148028http://purl.org/dc/terms/identifier"doi:10.1021/bi0021737"xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Sen U."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Sen U."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Varughese K.I."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Varughese K.I."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Vasudevan S."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Vasudevan S."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Ruggeri Z.M."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Ruggeri Z.M."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Celikel R."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Celikel R."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"McClintock R.A."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"McClintock R.A."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Subbarao G."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/author"Subbarao G."xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/pages"345-352"xsd:string
http://purl.uniprot.org/citations/11148028http://purl.uniprot.org/core/pages"345-352"xsd:string