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http://purl.uniprot.org/citations/20732303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20732303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20732303http://www.w3.org/2000/01/rdf-schema#comment"MKK4 activates both JNKs and p38s. We determined the crystal structures of human non-phosphorylated MKK4 kinase domain (npMKK4) complexed with AMP-PNP (npMKK4/AMP) and a ternary complex of npMKK4, AMP-PNP and p38α peptide (npMKK4/AMP/p38). These crystal structures revealed that the p38α peptide-bound npMKK4 at the allosteric site rather than at the putative substrate binding site and induced an auto-inhibition state. While the activation loop of the npMKK4/AMP complex was disordered, in the npMKK4/AMP/p38 complex it configured a long α-helix, which prevented substrate access to the active site and αC-helix movement to the active configuration of MKK4."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.08.071"xsd:string
http://purl.uniprot.org/citations/20732303http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.08.071"xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Hamada K."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Hamada K."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Matsumoto T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Matsumoto T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Yokota K."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Yokota K."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Tada T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Tada T."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Kirii Y."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/author"Kirii Y."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/pages"369-373"xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/pages"369-373"xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/title"Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state."xsd:string
http://purl.uniprot.org/citations/20732303http://purl.uniprot.org/core/title"Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state."xsd:string