7nr4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-RAY STRUCTURE OF PRMT6 IN COMPLEX WITH indazole type inhibitor== | |
| + | <StructureSection load='7nr4' size='340' side='right'caption='[[7nr4]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NR4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UO2:(2~{S})-2-azanyl-~{N}-[3-[3-(dimethylsulfamoyl)phenyl]-2~{H}-indazol-5-yl]propanamide'>UO2</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7nr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nr4 OCA], [https://pdbe.org/7nr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nr4 RCSB], [https://www.ebi.ac.uk/pdbsum/7nr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nr4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein arginine N-methyl transferase 4 (PRMT4) asymmetrically dimethylates the arginine residues of histone H3 and nonhistone proteins. The overexpression of PRMT4 in several cancers has stimulated interest in the discovery of inhibitors as biological tools and, potentially, therapeutics. Although several PRMT4 inhibitors have been reported, most display poor selectivity against other members of the PRMT family of methyl transferases. Herein, we report the structure-based design of a new class of alanine-containing 3-arylindoles as potent and selective PRMT4 inhibitors, and describe key structure-activity relationships for this class of compounds. | ||
| - | + | Rational Design and Synthesis of Selective PRMT4 Inhibitors: A New Chemotype for Development of Cancer Therapeutics*.,Sutherland M, Li A, Kaghad A, Panagopoulos D, Li F, Szewczyk M, Smil D, Scholten C, Bouche L, Stellfeld T, Arrowsmith CH, Barsyte D, Vedadi M, Hartung IV, Steuber H, Britton R, Santhakumar V ChemMedChem. 2021 Jan 29. doi: 10.1002/cmdc.202100018. PMID:33513288<ref>PMID:33513288</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Steuber | + | <div class="pdbe-citations 7nr4" style="background-color:#fffaf0;"></div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Steuber H]] | ||
Current revision
X-RAY STRUCTURE OF PRMT6 IN COMPLEX WITH indazole type inhibitor
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