Crystal structure of monkeypox H1 phosphatase, an antiviral drug target
Crystal structure of monkeypox H1 phosphatase, an antiviral drug target
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DOI：
10.1093/procel/pwac051
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发表时间：
2022
期刊：
影响因子：
21.1
通讯作者：
Wei Wang
中科院分区：
文献类型：
--
作者：
Wen Cui;Haojun Huang;Yinkai Duan;Zhi Luo;Haofeng Wang;Tenan Zhang;Henry C Nguyen;Wei Shen;Dan Su;Xi Li;Xiaoyun Ji;Haitao Yang;Wei Wang
Abstract. The current monkeypox outbreak has caused over 73,000 global cases, but the effective treatments are very limited. The dual specific phosphatase (H1) from monkeypox antagonizes the immune response and is crucial for viral replication, making it an attractive antiviral target. Here we determined a 1.8-Å crystal structure of H1, which forms a domain swapped dimer resembling a butterfly. Each active site, which consists of a Cys-Arg-Asp triad, captures a phosphate ion. The observed conformation mimics the final step of catalysis prior to product release. The crystal structure provides a strong foundation for the discovery of new antivirals against this emerging worldwide pathogen.
