The crystal structure of phosphorylated MAPK13 reveals common structural features and differences in p38 MAPK family activation

The p38 MAP kinases (p38 MAPKs) represent an important family centrally involved in mediating extracellular signaling. Recent studies indicate that family members such as MAPK13 (p38δ) display a selective cellular and tissue expression and are therefore involved in specific diseases. Detailed struct...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2015-04, Vol.71 (4), p.790-799
Hauptverfasser:	Yurtsever, Zeynep, Scheaffer, Suzanne M., Romero, Arthur G., Holtzman, Michael J., Brett, Tom J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation Amino Acid Sequence Binding Crystal structure Crystallization Crystallography, X-Ray Design engineering Enzyme Activation Humans Inhibitors Kinases MAPK13 Mitogen-Activated Protein Kinase 13 - chemistry Mitogen-Activated Protein Kinase 13 - metabolism Models, Molecular Molecular Sequence Data p38 MAP kinases p38 Mitogen-Activated Protein Kinases - chemistry p38 Mitogen-Activated Protein Kinases - metabolism Phosphorylation Protein Conformation Research Papers Residues Sequence Alignment Similarity
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