Mutagenesis of p38alpha MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-OUT state

In order to study the role of Phe169 in p38alpha MAP kinase structure and function, wild-type p38alpha and five p38alpha DFG motif mutants were examined in vitro for phosphorylation by MKK6, kinase activity toward ATF2 substrate, thermal stability, and X-ray crystal structure. All six p38alpha varia...

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Veröffentlicht in:	Biochemistry (Easton) 2007-05, Vol.46 (19), p.5687
Hauptverfasser:	Bukhtiyarova, Marina, Karpusas, Michael, Northrop, Katrina, Namboodiri, Haridasan V M, Springman, Eric B
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation Amino Acid Motifs Amino Acid Sequence CRYSTAL STRUCTURE Crystallization Crystallography, X-Ray Escherichia coli - metabolism FUNCTIONALS Hot Temperature IN VITRO MAP Kinase Kinase 6 - metabolism MATERIALS SCIENCE Mitogen-Activated Protein Kinase 14 - chemistry Mitogen-Activated Protein Kinase 14 - genetics Mitogen-Activated Protein Kinase 14 - metabolism MUTAGENESIS Mutagenesis, Site-Directed MUTANTS MUTATIONS national synchrotron light source PHENYLALANINE Phenylalanine - physiology PHOSPHORYLATION PHOSPHOTRANSFERASES Protein Conformation Protein Denaturation STABILITY
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