{"title":"一个结构开关揭示了如何解除USP30并解锁有丝分裂","authors":"Julia C. Fitzgerald, Anja Bremm","doi":"10.1038/s41594-025-01640-3","DOIUrl":null,"url":null,"abstract":"A recent high-resolution structure of USP30 bound to a selective inhibitor identifies a cryptic binding pocket formed through a conformational switch in the catalytic domain of the enzyme. This mechanistic insight opens a door to structure-guided design of mitophagy-enhancing compounds.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"21 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A structural switch reveals how to disarm USP30 and unlock mitophagy\",\"authors\":\"Julia C. Fitzgerald, Anja Bremm\",\"doi\":\"10.1038/s41594-025-01640-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"A recent high-resolution structure of USP30 bound to a selective inhibitor identifies a cryptic binding pocket formed through a conformational switch in the catalytic domain of the enzyme. This mechanistic insight opens a door to structure-guided design of mitophagy-enhancing compounds.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"21 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-07-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-025-01640-3\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-025-01640-3","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A structural switch reveals how to disarm USP30 and unlock mitophagy
A recent high-resolution structure of USP30 bound to a selective inhibitor identifies a cryptic binding pocket formed through a conformational switch in the catalytic domain of the enzyme. This mechanistic insight opens a door to structure-guided design of mitophagy-enhancing compounds.
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