A 2-Hydroxyisoquinoline-1,3-Dione Active-Site RNase H Inhibitor Binds in Multiple Modes to HIV-1 Reverse Transcriptase.

Citation data:

Antimicrobial agents and chemotherapy, ISSN: 1098-6596, Vol: 61, Issue: 10, Page: e01351-17

Publication Year:
2017
Usage 2
Abstract Views 2
Citations 1
Citation Indexes 1
PMID:
28760905
DOI:
10.1128/aac.01351-17
Author(s):
Kirby, Karen A, Myshakina, Nataliya A, Christen, Martin T, Chen, Yue-Lei, Schmidt, Hilary A, Huber, Andrew D, Xi, Zhaoyong, Kim, Seongmi, Rao, Rohit K, Kramer, Skyler T, Yang, Qiongying, Singh, Kamalendra, Parniak, Michael A, Wang, Zhengqiang, Ishima, Rieko, Sarafianos, Stefan G Show More Hide
Publisher(s):
American Society for Microbiology
Tags:
Pharmacology, Toxicology and Pharmaceutics, Medicine
article description
The RNase H (RNH) function of HIV-1 reverse transcriptase (RT) plays an essential part in the viral life cycle. We report the characterization of YLC2-155, a 2-hydroxyisoquinoline-1,3-dione (HID)-based active-site RNH inhibitor. YLC2-155 inhibits both polymerase (50% inhibitory concentration [IC] = 2.6 μM) and RNH functions (IC = 0.65 μM) of RT but is more effective against RNH. X-ray crystallography, nuclear magnetic resonance (NMR) analysis, and molecular modeling were used to show that YLC2-155 binds at the RNH-active site in multiple conformations.

This article has 0 Wikipedia mention.