化学
RNA聚合酶
抗菌剂
聚合酶
细菌蛋白
药物发现
蛋白质-蛋白质相互作用
核糖核酸
计算生物学
生物化学
酶
基因
生物
有机化学
作者
Yingbo Zheng,Cheuk Hei Kan,Tsz Fung Tsang,Yanpeng Liu,T.Y. Liu,Man Wai Tsang,Long Yin Lam,Xiao Yang,Cong Ma
标识
DOI:10.1021/acs.jmedchem.4c01386
摘要
Bacterial RNA polymerase (RNAP), the core enzyme responsible for bacterial transcription, requires the NusG factor for efficient transcription elongation and termination. As the primary binding site for NusG, the RNAP clamp-helix (CH) domain represents a potential protein-protein interaction (PPI) target for novel antimicrobial agent design and discovery. In this study, we designed a pharmacophore model based on the essential amino acids of the CH for binding to NusG, such as R270, R278, and R281 (
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