2OKR
Crystal Structure of the P38a-MAPKAP kinase 2 Heterodimer
Summary for 2OKR
| Entry DOI | 10.2210/pdb2okr/pdb |
| Related | 2ONL |
| Descriptor | Mitogen-activated protein kinase 14, MAP kinase-activated protein kinase 2 (3 entities in total) |
| Functional Keywords | kinase, nls, nes, heterodimer, docking groove, transferase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm (By similarity): Q16539 |
| Total number of polymer chains | 4 |
| Total formula weight | 89622.90 |
| Authors | Ter Haar, E. (deposition date: 2007-01-17, release date: 2007-02-06, Last modification date: 2023-08-30) |
| Primary citation | ter Haar, E.,Prabakhar, P.,Liu, X.,Lepre, C. Crystal structure of the P38alpha-MAPKAP kinase 2 heterodimer. J.Biol.Chem., 282:9733-9739, 2007 Cited by PubMed Abstract: The p38 signaling pathway is activated in response to cell stress and induces production of proinflammatory cytokines. P38alpha is phosphorylated and activated in response to cell stress by MKK3 and MKK6 and in turn phosphorylates a number of substrates, including MAPKAP kinase 2 (MK2). We have determined the crystal structure of the unphosphorylated p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in the docking groove of p38alpha, and the ATP-binding sites of both kinases are at the heterodimer interface. The conformation suggests an extra mechanism in addition to the regulation of the p38alpha and MK2 phosphorylation states that prevents phosphorylation of substrates in the absence of cell stress. Addition of constitutively active MKK6-DD results in rapid phosphorylation of the p38alpha-MK2 heterodimer. PubMed: 17255097DOI: 10.1074/jbc.M611165200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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