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http://purl.uniprot.org/citations/18597489http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18597489http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18597489http://www.w3.org/2000/01/rdf-schema#comment"Aggretin is a C-type lectin purified from Calloselasma rhodostoma snake venom. It is a potent activator of platelets, resulting in a collagen-like response by binding and clustering platelet receptor CLEC-2. We present here the crystal structure of aggretin at 1.7 A which reveals a unique tetrameric quaternary structure. The two alphabeta heterodimers are arranged through 2-fold rotational symmetry, resulting in an antiparallel side-by-side arrangement. Aggretin thus presents two ligand binding sites on one surface and can therefore cluster ligands in a manner reminiscent of convulxin and flavocetin. To examine the molecular basis of the interaction with CLEC-2, we used a molecular modeling approach of docking the aggretin alphabeta structure with the CLEC-2 N-terminal domain (CLEC-2N). This model positions the CLEC-2N structure face down in the "saddle"-shaped binding site which lies between the aggretin alpha and beta lectin-like domains. A 2-fold rotation of this complex to generate the aggretin tetramer reveals dimer contacts for CLEC-2N which bring the N- and C-termini into the proximity of each other, and a series of contacts involving two interlocking beta-strands close to the N-terminus are described. A comparison with homologous lectin-like domains from the immunoreceptor family reveals a similar but not identical dimerization mode, suggesting this structure may represent the clustered form of CLEC-2 capable of signaling across the platelet membrane."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.org/dc/terms/identifier"doi:10.1021/bi800528t"xsd:string
http://purl.uniprot.org/citations/18597489http://purl.org/dc/terms/identifier"doi:10.1021/bi800528t"xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Papagrigoriou E."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Papagrigoriou E."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Clemetson K.J."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Clemetson K.J."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Pandey A.V."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Pandey A.V."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Emsley J."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Emsley J."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Clemetson J.M."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Clemetson J.M."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Navdaev A."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Navdaev A."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Hooley E."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/author"Hooley E."xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/pages"7831-7837"xsd:string
http://purl.uniprot.org/citations/18597489http://purl.uniprot.org/core/pages"7831-7837"xsd:string