当前位置: X-MOL 学术Science › 论文详情
Structural basis for strand-transfer inhibitor binding to HIV intasomes
Science ( IF 41.037 ) Pub Date : 2020-02-14 , DOI: 10.1126/science.aay8015
Dario Oliveira Passos, Min Li, Ilona K. Jóźwik, Xue Zhi Zhao, Diogo Santos-Martins, Renbin Yang, Steven J. Smith, Youngmin Jeon, Stefano Forli, Stephen H. Hughes, Terrence R. Burke, Robert Craigie, Dmitry Lyumkis

The HIV intasome is a large nucleoprotein assembly that mediates the integration of a DNA copy of the viral genome into host chromatin. Intasomes are targeted by the latest generation of antiretroviral drugs, integrase strand-transfer inhibitors (INSTIs). Challenges associated with lentiviral intasome biochemistry have hindered high-resolution structural studies of how INSTIs bind to their native drug target. Here, we present high-resolution cryo–electron microscopy structures of HIV intasomes bound to the latest generation of INSTIs. These structures highlight how small changes in the integrase active site can have notable implications for drug binding and design and provide mechanistic insights into why a leading INSTI retains efficacy against a broad spectrum of drug-resistant variants. The data have implications for expanding effective treatments available for HIV-infected individuals.
更新日期:2020-02-13

 

全部期刊列表>>
Springer Nature 2019高下载量文章和章节
化学/材料学中国作者研究精选
《科学报告》最新环境科学研究
ACS材料视界
自然科研论文编辑服务
中南大学国家杰青杨华明
剑桥大学-
中南大学
材料化学和生物传感方向博士后招聘
课题组网站
X-MOL
北京大学分子工程苏南研究院
华东师范大学分子机器及功能材料
中山大学化学工程与技术学院
试剂库存
天合科研
down
wechat
bug