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http://purl.uniprot.org/citations/9891971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9891971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9891971http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9891971http://www.w3.org/2000/01/rdf-schema#comment"We show by site-directed mutagenesis that the catalytic residues of mammalian legumain, a recently discovered lysosomal asparaginycysteine endopeptidase, form a catalytic dyad in the motif His-Gly-spacer-Ala-Cys. We note that the same motif is present in the caspases, aspartate-specific endopeptidases central to the process of apoptosis in animal cells, and also in the families of clostripain and gingipain which are arginyl/lysyl endopeptidases of pathogenic bacteria. We propose that the four families have similar protein folds, are evolutionarily related in clan CD, and have common characteristics including substrate specificities dominated by the interactions of the S1 subsite."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01574-9"xsd:string
http://purl.uniprot.org/citations/9891971http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01574-9"xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Barrett A.J."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Barrett A.J."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Rawlings N.D."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Rawlings N.D."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Chen J.-M."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Chen J.-M."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Stevens R.A."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/author"Stevens R.A."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/pages"361-365"xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/pages"361-365"xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/title"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/title"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases."xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/volume"441"xsd:string
http://purl.uniprot.org/citations/9891971http://purl.uniprot.org/core/volume"441"xsd:string
http://purl.uniprot.org/citations/9891971http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9891971