4ijp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 10: | Line 10: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ijp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ijp RCSB], [http://www.ebi.ac.uk/pdbsum/4ijp PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ijp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ijp RCSB], [http://www.ebi.ac.uk/pdbsum/4ijp PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PRP4B_HUMAN PRP4B_HUMAN]] Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 09:40, 25 December 2014
Crystal Structure of Human PRPF4B kinase domain in complex with 4-{5-[(2-Chloro-pyridin-4-ylmethyl)-carbamoyl]-thiophen-2-yl}-benzo[b]thiophene-2-carboxylic acid amineCrystal Structure of Human PRPF4B kinase domain in complex with 4-{5-[(2-Chloro-pyridin-4-ylmethyl)-carbamoyl]-thiophen-2-yl}-benzo[b]thiophene-2-carboxylic acid amine
Structural highlights
Function[PRP4B_HUMAN] Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. Publication Abstract from PubMedPRP4 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. Evaluation of cancer dependence and druggability of PRP4 kinase using cellular, biochemical, and structural approaches.,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 SM J Biol Chem. 2013 Sep 3. PMID:24003220[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||||||