7NR4
X-RAY STRUCTURE OF PRMT6 IN COMPLEX WITH indazole type inhibitor
Summary for 7NR4
| Entry DOI | 10.2210/pdb7nr4/pdb |
| Descriptor | Protein arginine N-methyltransferase 6, S-ADENOSYL-L-HOMOCYSTEINE, (2~{S})-2-azanyl-~{N}-[3-[3-(dimethylsulfamoyl)phenyl]-2~{H}-indazol-5-yl]propanamide, ... (4 entities in total) |
| Functional Keywords | protein arginine methyl transferase 6, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 171385.70 |
| Authors | Steuber, H. (deposition date: 2021-03-02, release date: 2021-04-07, Last modification date: 2024-01-31) |
| Primary citation | Sutherland, M.,Li, A.,Kaghad, A.,Panagopoulos, D.,Li, F.,Szewczyk, M.,Smil, D.,Scholten, C.,Bouche, L.,Stellfeld, T.,Arrowsmith, C.H.,Barsyte, D.,Vedadi, M.,Hartung, I.V.,Steuber, H.,Britton, R.,Santhakumar, V. Rational Design and Synthesis of Selective PRMT4 Inhibitors: A New Chemotype for Development of Cancer Therapeutics*. Chemmedchem, 16:1116-1125, 2021 Cited by PubMed Abstract: 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. PubMed: 33513288DOI: 10.1002/cmdc.202100018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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