4IIR
Crystal Structure of AMPPNP-bound Human PRPF4B kinase domain
Summary for 4IIR
| Entry DOI | 10.2210/pdb4iir/pdb |
| Related | 4IAN 4IFC 4IJP |
| Descriptor | Serine/threonine-protein kinase PRP4 homolog, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | kinase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q13523 |
| Total number of polymer chains | 2 |
| Total formula weight | 85287.89 |
| Authors | Mechin, I.,Haas, K.,Chen, X.,Zhang, Y.,McLean, L. (deposition date: 2012-12-20, release date: 2013-08-28, Last modification date: 2017-11-15) |
| Primary citation | Gao, Q.,Mechin, I.,Kothari, N.,Guo, Z.,Deng, G.,Haas, K.,McManus, J.,Hoffmann, D.,Wang, A.,Wiederschain, D.,Rocnik, J.,Czechtizky, W.,Chen, X.,McLean, L.,Arlt, H.,Harper, D.,Liu, F.,Majid, T.,Patel, V.,Lengauer, C.,Garcia-Echeverria, C.,Zhang, B.,Cheng, H.,Dorsch, M.,Huang, S.M. Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches. J.Biol.Chem., 288:30125-30138, 2013 Cited by PubMed Abstract: PRP4 kinase is known for its roles in regulating pre-mRNA splicing and beyond. Therefore, a wider spectrum of PRP4 kinase substrates could be expected. The role of PRP4 kinase in cancer is also yet to be fully elucidated. Attaining specific and potent PRP4 inhibitors would greatly facilitate the study of PRP4 biological function and its validation as a credible cancer target. In this report, we verified the requirement of enzymatic activity of PRP4 in regulating cancer cell growth and identified an array of potential novel substrates through orthogonal proteomics approaches. The ensuing effort in structural biology unveiled for the first time unique features of PRP4 kinase domain and its potential mode of interaction with a low molecular weight inhibitor. These results provide new and important information for further exploration of PRP4 kinase function in cancer. PubMed: 24003220DOI: 10.1074/jbc.M113.473348 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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