@article {Cui2022.09.30.510410, author = {Wen Cui and Haojun Huang and Yinkai Duan and Zhi Luo and Haofeng Wang and Tenan Zhang and Henry Nguyen and Wei Shen and Dan Su and Xiaoyun Ji and Haitao Yang and Wei Wang}, title = {Crystal structure of monkeypox H1 phosphatase, an Antiviral Drug Target}, elocation-id = {2022.09.30.510410}, year = {2022}, doi = {10.1101/2022.09.30.510410}, publisher = {Cold Spring Harbor Laboratory}, abstract = {The current monkeypox outbreak has caused over 64,000 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-{\r A} 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.Competing Interest StatementThe authors have declared no competing interest.}, URL = {https://www.biorxiv.org/content/early/2022/10/03/2022.09.30.510410}, eprint = {https://www.biorxiv.org/content/early/2022/10/03/2022.09.30.510410.full.pdf}, journal = {bioRxiv} }