4IFC

Crystal Structure of ADP-bound Human PRPF4B kinase domain

4IFC の概要

• エントリーDOI: 10.2210/pdb4ifc/pdb
• 関連するPDBエントリー: 4IAN 4IIR 4IJP
• 分子名称: Serine/threonine-protein kinase PRP4 homolog, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: kinase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q13523
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85009.53

構造登録者

Mechin, I.,Haas, K.,Chen, X.,Zhang, Y.,McLean, L. (登録日: 2012-12-14, 公開日: 2013-08-28, 最終更新日: 2024-10-16)

主引用文献

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

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: 24003220
DOI: 10.1074/jbc.M113.473348

実験手法

X-RAY DIFFRACTION (2.13 Å)