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http://purl.uniprot.org/citations/15728581http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15728581http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15728581http://www.w3.org/2000/01/rdf-schema#comment"Cystatins are natural inhibitors of papain-like (family C1) and legumain-related (family C13) cysteine peptidases. Cystatin D is a type 2 cystatin, a secreted inhibitor found in human saliva and tear fluid. Compared with its homologues, cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain. To elucidate the structural reasons for this specificity, we have crystallized recombinant human Arg(26)-cystatin D and solved its structures at room temperature and at cryo conditions to 2.5- and 1.8-A resolution, respectively. Human cystatin D presents the typical cystatin fold, with a five-stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix. The structures reveal differences in the peptidase-interacting regions when compared with other cystatins, providing plausible explanations for the restricted inhibitory specificity of cystatin D for some papain-like peptidases and its lack of reactivity toward legumain-related enzymes."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411914200"xsd:string
http://purl.uniprot.org/citations/15728581http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411914200"xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Abrahamson M."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Abrahamson M."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Alvarez-Fernandez M."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Alvarez-Fernandez M."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Su X.D."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Su X.D."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Liang Y.H."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/author"Liang Y.H."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/pages"18221-18228"xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/pages"18221-18228"xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/title"Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/title"Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile."xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15728581http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15728581http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15728581
http://purl.uniprot.org/citations/15728581http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15728581