4BFM
The crystal structure of mouse PK38
Summary for 4BFM
| Entry DOI | 10.2210/pdb4bfm/pdb |
| Descriptor | MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Cellular location | Cell membrane; Peripheral membrane protein (By similarity): Q61846 |
| Total number of polymer chains | 1 |
| Total formula weight | 39823.39 |
| Authors | Yoo, J.H.,Cho, Y.S.,Park, S.M.,Cho, H.S. (deposition date: 2013-03-21, release date: 2014-02-12, Last modification date: 2023-12-20) |
| Primary citation | Cho, Y.S.,Yoo, J.,Park, S.,Cho, H.S. The Structures of the Kinase Domain and Uba Domain of Mpk38 Suggest the Activation Mechanism for Kinase Activity. Acta Crystallogr.,Sect.D, 70:514-, 2014 Cited by PubMed Abstract: Murine protein serine/threonine kinase 38 (MPK38) is the murine orthologue of human maternal embryonic leucine-zipper kinase (MELK), which belongs to the SNF1/AMPK family. MELK is considered to be a promising drug target for anticancer therapy because overexpression and hyperactivation of MELK is correlated with several human cancers. Activation of MPK38 requires the extended sequence (ExS) containing the ubiquitin-associated (UBA) linker and UBA domain and phosphorylation of the activation loop. However, the activation mechanism of MPK38 is unknown. This paper reports the crystal structure of MPK38 (T167E), which mimics a phosphorylated state of the activation loop, in complex with AMP-PNP. In the MPK38 structure, the UBA linker forces an inward movement of the αC helix. Phosphorylation of the activation loop then induces movement of the activation loop towards the C-lobe and results in interlobar cleft closure. These processes generate a fully active state of MPK38. This structure suggests that MPK38 has a similar molecular mechanism regulating activation as in other kinases of the SNF1/AMPK family. PubMed: 24531485DOI: 10.1107/S1399004713027806 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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