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http://purl.uniprot.org/citations/16236260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16236260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16236260http://www.w3.org/2000/01/rdf-schema#comment"AMP-activated protein kinase (AMPK) is a master metabolic regulator, and is an important target for drug development against diabetes, obesity, and other diseases. AMPK is a hetero-trimeric enzyme, with a catalytic (alpha) subunit, and two regulatory (beta and gamma) subunits. Here we report the crystal structure at 2.2A resolution of the protein kinase domain (KD) of the catalytic subunit of yeast AMPK (commonly known as SNF1). The Snf1-KD structure shares strong similarity to other protein kinases, with a small N-terminal lobe and a large C-terminal lobe. Two negative surface patches in the structure may be important for the recognition of the substrates of this kinase."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2005.09.181"xsd:string
http://purl.uniprot.org/citations/16236260http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2005.09.181"xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Tong L."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Tong L."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Rudolph M.J."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Rudolph M.J."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Amodeo G.A."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/author"Amodeo G.A."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/pages"1224-1228"xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/pages"1224-1228"xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/title"Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/title"Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1."xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/volume"337"xsd:string
http://purl.uniprot.org/citations/16236260http://purl.uniprot.org/core/volume"337"xsd:string
http://purl.uniprot.org/citations/16236260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16236260
http://purl.uniprot.org/citations/16236260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16236260