变构调节：动力学是双刃剑。
Allosteric Modulation: Dynamics is Double-"E"dged.
机构信息
Department of Medicinal Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Zhangjiang Hi-Tech Park, Shanghai 201203, P.R. China.
出版信息
J Med Chem. 2021 Apr 8;64(7):3694-3696. doi: 10.1021/acs.jmedchem.1c00473. Epub 2021 Mar 24.
Protein arginine methyltransferase 6 (PRMT6), a member of type I PRMT enzymes, catalyzes the monomethylation or asymmetric dimethylation of arginine residues. To better understand its biological roles in cells, highly selective inhibitors are needed. The first reported allosteric inhibitor of PRMT6 should fulfill this need. Further comparison with allosteric inhibitors of PRMT5 identified that the dynamics of double-E loop plays a vital role in making this allosteric binding possible.
精氨酸甲基转移酶 6（PRMT6）是 I 型 PRMT 酶的成员，可催化精氨酸残基的单甲基化或非对称二甲基化。为了更好地理解其在细胞中的生物学作用，需要高度选择性的抑制剂。第一个报道的 PRMT6 的别构抑制剂应该满足这一需求。与 PRMT5 的别构抑制剂的进一步比较表明，双 E 环的动力学在使这种别构结合成为可能方面起着至关重要的作用。
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