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http://purl.uniprot.org/citations/21423620http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21423620http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21423620http://www.w3.org/2000/01/rdf-schema#comment"In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-terminal extension with the edge of the lectin site are consistently observed, revealing a hitherto unidentified peptide-binding site. A calreticulin molecular zipper, observed in all crystal lattices, could further extend this site by creating a binding cavity lined by hydrophobic residues. These data thus provide a first structural insight into the lectin-independent binding properties of calreticulin and suggest new working hypotheses, including that of a multi-molecular mechanism."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0017886"xsd:string
http://purl.uniprot.org/citations/21423620http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0017886"xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Chouquet A."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Chouquet A."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Gaboriaud C."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Gaboriaud C."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Arlaud G.J."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Arlaud G.J."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Ling W.L."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Ling W.L."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Houen G."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Houen G."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Frachet P."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Frachet P."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Paidassi H."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/author"Paidassi H."xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/pages"E17886"xsd:string
http://purl.uniprot.org/citations/21423620http://purl.uniprot.org/core/pages"E17886"xsd:string