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http://purl.uniprot.org/citations/16601115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16601115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16601115http://www.w3.org/2000/01/rdf-schema#comment"Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase. Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes. It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile. We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state. The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation. Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m601033200"xsd:string
http://purl.uniprot.org/citations/16601115http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m601033200"xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Schuettelkopf A.W."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Schuettelkopf A.W."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"van Aalten D.M.F."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"van Aalten D.M.F."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Watts C."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Watts C."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Hamilton G."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/author"Hamilton G."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/pages"16570-16575"xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/pages"16570-16575"xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/title"Structural basis of reduction-dependent activation of human cystatin F."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/title"Structural basis of reduction-dependent activation of human cystatin F."xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16601115http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16601115http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16601115
http://purl.uniprot.org/citations/16601115http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16601115