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http://purl.uniprot.org/citations/15006348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15006348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15006348http://www.w3.org/2000/01/rdf-schema#comment"Hematophagous arthropods secrete a salivary apyrase that inhibits platelet activation by catabolizing ADP released from damaged tissues and blood cells. We report the X-ray crystal structures of a human enzyme of the soluble apyrase family in its apo state and bound to a substrate analog. The structures reveal a nucleotide binding domain comprising a five-blade beta propeller, binding determinants of the substrate and the active site, and an unusual calcium binding site with a potential regulatory function. Using a comparative structural biology approach, we were able to redesign the human apyrase so as to enhance its ADPase activity by more than 100-fold. The engineered enzyme is a potent inhibitor of platelet aggregation and may serve as the basis for the development of a new class of antithrombotic agents."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(04)00172-2"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(04)00172-2"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Deng Y."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Deng Y."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Lu M."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Lu M."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Smith T.M."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Smith T.M."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Dai J."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/author"Dai J."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/pages"649-659"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/pages"649-659"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/title"Structure and protein design of a human platelet function inhibitor."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/title"Structure and protein design of a human platelet function inhibitor."xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/volume"116"xsd:string
http://purl.uniprot.org/citations/15006348http://purl.uniprot.org/core/volume"116"xsd:string