| Literature DB >> 24003220 |
Qiang Gao1, Ingrid Mechin, Nayantara Kothari, Zhuyan Guo, Gejing Deng, Kimberly Haas, Jessica McManus, Dietmar Hoffmann, Anlai Wang, Dmitri Wiederschain, Jennifer Rocnik, Werngard Czechtizky, Xin Chen, Larry McLean, Heike Arlt, David Harper, Feng Liu, Tahir Majid, Vinod Patel, Christoph Lengauer, Carlos Garcia-Echeverria, Bailin Zhang, Hong Cheng, Marion Dorsch, Shih-Min A Huang.
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.Entities:
Keywords: Cancer Therapy; Crystallography; Drug Discovery; Proteomics; Structural Biology
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Year: 2013 PMID： 24003220 PMCID： PMC3798481 DOI： 10.1074/jbc.M113.473348
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157