RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/20124694http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20124694http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20124694http://www.w3.org/2000/01/rdf-schema#comment"The MST family is a subclass of mammalian serine/threonine kinases that are related to the yeast sterile-20 protein and are implicated in regulating cell growth and transformation. The MST3 protein contains a 300-residue catalytic domain and a 130-residue regulatory domain, which can be cleaved by caspase and activated by autophosphorylation, promoting apoptosis. Here, five crystal structures of the catalytic domain of MST3 are presented, including a complex with ADP and manganese, a unique cofactor preferred by the enzyme, and a complex with adenine. Similar to other protein kinases, the catalytic domain of MST3 folds into two lobes: the smaller N lobe forms the nucleotide-binding site and the larger C lobe recognizes the polypeptide substrate. The bound ADP and Mn(2+) ions are covered by a glycine-rich loop and held in place by Asn149 and Asp162. A different orientation was observed for the ligand in the MST3-adenine complex. In the activation loop, the side chain of Thr178 is phosphorylated and is sandwiched by Arg143 and Arg176. Comparison of this structure with other similar kinase structures shows a 180 degrees rotation of the loop, leading to activation of the enzyme. The well defined protein-ligand interactions also provide useful information for the design of potent inhibitors."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.org/dc/terms/identifier"doi:10.1107/s0907444909047507"xsd:string
http://purl.uniprot.org/citations/20124694http://purl.org/dc/terms/identifier"doi:10.1107/s0907444909047507"xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Ko T.P."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Ko T.P."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Wang A.H."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Wang A.H."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Liu C.I."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Liu C.I."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Chang W.J."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Chang W.J."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Lai M.D."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Lai M.D."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Wu C.L."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Wu C.L."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Jeng W.Y."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Jeng W.Y."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Shr H.L."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Shr H.L."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Lu T.J."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/author"Lu T.J."xsd:string
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20124694http://purl.uniprot.org/core/date"2010"xsd:gYear