| http://purl.uniprot.org/citations/18977227 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18977227 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18977227 | http://www.w3.org/2000/01/rdf-schema#comment | "Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human-brain-type-creatine-kinase (hBB-CK) were identified by X-ray crystallography: the ligand-free-form at 2.2A; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0A. The structures of ligand-bound hBB-CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP-Mg2+-complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP-Mg2+ alone may trigger conformational changes in hBB-CK that were not observed with muscle-type-CK."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2008.10.039"xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2008.10.039"xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Lee K.S."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Lee K.S."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Hwang K.Y."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Hwang K.Y."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Moon J.H."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Moon J.H."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Nam K.H."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Nam K.H."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Chi Y.M."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Chi Y.M."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Bong S.M."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/author | "Bong S.M."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/pages | "3959-3965"xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/pages | "3959-3965"xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/title | "Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex."xsd:string |
| http://purl.uniprot.org/citations/18977227 | http://purl.uniprot.org/core/title | "Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex."xsd:string |