| http://purl.uniprot.org/citations/21543851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21543851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21543851 | http://www.w3.org/2000/01/rdf-schema#comment | "AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels and is therefore a potential target for drug design against metabolic syndrome, obesity and type 2 diabetes. Here, the crystal structure of the phosphorylated-state mimic T172D mutant kinase domain from the human AMPK α2 subunit is reported in the apo form and in complex with a selective inhibitor, compound C. The AMPK α2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the `DFG-out' conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket. Compound C binding dramatically alters the conformation of the activation loop, which adopts an intermediate conformation between DFG-out and DFG-in. This induced fit forms a compound-C binding pocket composed of the N-lobe, the C-lobe and the hinge of the kinase domain. The pocket partially overlaps with the putative ATP-binding pocket. These three-dimensional structures will be useful to guide drug discovery."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444911010201"xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444911010201"xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Kishishita S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Kishishita S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Lee S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Lee S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Shirouzu M."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Shirouzu M."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Terada T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Terada T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Suzuki A."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Suzuki A."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Yokoyama S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Yokoyama S."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Takagi T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Takagi T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Kadowaki T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Kadowaki T."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Handa N."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Handa N."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Iwabu M."xsd:string |
| http://purl.uniprot.org/citations/21543851 | http://purl.uniprot.org/core/author | "Iwabu M."xsd:string |