| http://purl.uniprot.org/citations/20823513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20823513 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20823513 | http://www.w3.org/2000/01/rdf-schema#comment | "AMP-activated protein kinase (AMPK) is a master metabolic regulator for controlling cellular energy homeostasis. Its homolog in yeast, SNF1, is activated in response to glucose depletion and other stresses. The catalytic (alpha) subunit of AMPK/SNF1 in yeast (Snf1) contains a protein Ser/Thr kinase domain (KD), an auto-inhibitory domain (AID) and a region that mediates interactions with the two regulatory (beta and gamma) subunits. Here, the crystal structure of residues 41-440 of Snf1, which include the KD and AID, is reported at 2.4 A resolution. The AID is completely disordered in the crystal. A new inhibited conformation of the KD is observed in a DFG-out conformation and with the glycine-rich loop adopting a structure that blocks ATP binding to the active site."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.org/dc/terms/identifier | "doi:10.1107/s1744309110028265"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.org/dc/terms/identifier | "doi:10.1107/s1744309110028265"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Tong L."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Tong L."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Rudolph M.J."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Rudolph M.J."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Amodeo G.A."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/author | "Amodeo G.A."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/name | "Acta Crystallogr. F"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/name | "Acta Crystallogr. F"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/pages | "999-1002"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/pages | "999-1002"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/title | "An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/title | "An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1."xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/volume | "66"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://purl.uniprot.org/core/volume | "66"xsd:string |
| http://purl.uniprot.org/citations/20823513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20823513 |
| http://purl.uniprot.org/citations/20823513 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20823513 |
| http://purl.uniprot.org/citations/20823513 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20823513 |
| http://purl.uniprot.org/citations/20823513 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20823513 |