{"title":"基于gid4蛋白水解靶向嵌合体降解机制的研究","authors":"","doi":"10.1038/s41594-025-01539-z","DOIUrl":null,"url":null,"abstract":"The Pro/N-degron E3 ligase GID4 can be harnessed for proteolysis-targeting chimera (PROTAC) applications, as demonstrated by a GID4-based bromodomain-containing protein 4 (BRD4)-targeting PROTAC, which inhibits cell proliferation and exhibits antitumor activity. Structural analysis of the GID4–PROTAC–BRD4 ternary complexes reveals plasticity in the underlying interactions, providing valuable insights into the degradation mechanism.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"52 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Insights into the degradation mechanism of GID4-based proteolysis-targeting chimeras\",\"authors\":\"\",\"doi\":\"10.1038/s41594-025-01539-z\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The Pro/N-degron E3 ligase GID4 can be harnessed for proteolysis-targeting chimera (PROTAC) applications, as demonstrated by a GID4-based bromodomain-containing protein 4 (BRD4)-targeting PROTAC, which inhibits cell proliferation and exhibits antitumor activity. Structural analysis of the GID4–PROTAC–BRD4 ternary complexes reveals plasticity in the underlying interactions, providing valuable insights into the degradation mechanism.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"52 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-05-15\",\"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/s41594-025-01539-z\",\"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/s41594-025-01539-z","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Insights into the degradation mechanism of GID4-based proteolysis-targeting chimeras
The Pro/N-degron E3 ligase GID4 can be harnessed for proteolysis-targeting chimera (PROTAC) applications, as demonstrated by a GID4-based bromodomain-containing protein 4 (BRD4)-targeting PROTAC, which inhibits cell proliferation and exhibits antitumor activity. Structural analysis of the GID4–PROTAC–BRD4 ternary complexes reveals plasticity in the underlying interactions, providing valuable insights into the degradation mechanism.
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