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http://purl.uniprot.org/citations/14656436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14656436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14656436http://www.w3.org/2000/01/rdf-schema#comment"The two Ca2+-dependent cysteine proteases, micro- and m-calpain, are involved in various Ca2+-linked signal pathways but differ markedly in their Ca2+ requirements for activation. We have determined the structure of a micro-like calpain, which has 85% micro-calpain sequence (the first 48 and the last 62 residues of the large subunit are those from m-calpain) and a low Ca2+ requirement. This construct was used because micro-calpain itself is too poorly expressed. The structure of micro-like calpain is very similar in overall fold to that of m-calpain as expected, but differs significantly in two aspects. In comparison with m-calpain, the catalytic triad residues in micro-like calpain, His and Cys, are much closer together in the absence of Ca2+, and significant portions of the Ca2+ binding EF-hand motifs are disordered and more flexible. These structural differences imply that Ca2+-free micro-calpain may represent a partially activated structure, requiring lower Ca2+ concentration to trigger its activation."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2003.11.007"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2003.11.007"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Jia Z."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Jia Z."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Pal G.P."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Pal G.P."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"De Veyra T."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"De Veyra T."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Elce J.S."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/author"Elce J.S."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/pages"1521-1526"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/pages"1521-1526"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/title"Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/title"Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement."xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/14656436http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/14656436http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14656436
http://purl.uniprot.org/citations/14656436http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14656436