4CQG
The crystal structure of MPK38 in complex with OTSSP167, an orally- administrative MELK selective inhibitor
Summary for 4CQG
| Entry DOI | 10.2210/pdb4cqg/pdb |
| Descriptor | Maternal embryonic leucine zipper kinase, 1-[6-(3,5-dichloro-4-hydroxyphenyl)-4-({trans-4-[(dimethylamino)methyl]cyclohexyl}amino)-1,5-naphthyridin-3-yl]ethanone, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 38909.86 |
| Authors | Cho, Y.S.,Kang, Y.J.,Cho, H.S. (deposition date: 2014-02-17, release date: 2014-07-09, Last modification date: 2023-12-20) |
| Primary citation | Cho, Y.S.,Kang, Y.,Kim, K.,Cha, Y.J.,Cho, H.S. The crystal structure of MPK38 in complex with OTSSP167, an orally administrative MELK selective inhibitor. Biochem.Biophys.Res.Commun., 447:7-11, 2014 Cited by PubMed Abstract: Murine protein serine/threonine kinase 38 (MPK38), also known as maternal embryonic leucine zipper kinase (MELK), has been associated with various human cancers and plays an important role in the formation of cancer stem cells. OTSSP167, a MELK selective inhibitor, exhibits a strong in vitro activity, conferring an IC50 of 0.41nM and in vivo effect on various human cancer xenograft models. Here, we report the crystal structure of MPK38 (T167E), an active mutant, in complex with OTSSP167 and describe its detailed protein-inhibitor interactions. Comparison with the previous determined structure of MELK bound to the nanomolar inhibitors shows that OTSSP167 effectively fits into the active site, thus offering an opportunity for structure-based development and optimization of MELK inhibitors. PubMed: 24657156DOI: 10.1016/j.bbrc.2014.03.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
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