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http://purl.uniprot.org/citations/18583525http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18583525http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18583525http://www.w3.org/2000/01/rdf-schema#comment"Binding of the snake venom protein rhodocytin to CLEC-2, a receptor on the surface of human platelets, initiates a signaling cascade leading to platelet activation and aggregation. We have previously solved the structure of CLEC-2. The 2.4 A resolution crystal structure of rhodocytin presented here demonstrates that it is the first snake venom or other C-type lectin-like protein to assemble as a non-disulfide linked (alphabeta)(2) tetramer. Rhodocytin is highly adapted for interaction with CLEC-2 and displays a concave binding surface, which is highly complementary to the experimentally determined binding interface on CLEC-2. Using computational dynamic methods, surface electrostatic charge and hydrophobicity analyses, and protein-protein docking predictions, we propose that the (alphabeta)(2) rhodocytin tetramer induces clustering of CLEC-2 receptors on the platelet surface, which will trigger major signaling events resulting in platelet activation and aggregation."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.org/dc/terms/identifier"doi:10.1110/ps.035568.108"xsd:string
http://purl.uniprot.org/citations/18583525http://purl.org/dc/terms/identifier"doi:10.1110/ps.035568.108"xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"Watson A.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"Watson A.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"Eble J.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"Eble J.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"O'Callaghan C.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/author"O'Callaghan C.A."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/pages"1611-1616"xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/pages"1611-1616"xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/title"Crystal structure of rhodocytin, a ligand for the platelet-activating receptor CLEC-2."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/title"Crystal structure of rhodocytin, a ligand for the platelet-activating receptor CLEC-2."xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/18583525http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/18583525http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18583525
http://purl.uniprot.org/citations/18583525http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18583525
http://purl.uniprot.org/citations/18583525http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18583525
http://purl.uniprot.org/citations/18583525http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18583525