{"title":"FN3K:最甜的激酶。","authors":"Joyce Ogidigo , Reena Kumari , Viraj R. Sanghvi","doi":"10.1016/j.tibs.2025.03.009","DOIUrl":null,"url":null,"abstract":"<div><div>Fructosamine 3-kinase (FN3K) mitigates excessive protein glycation by phosphorylating and destabilizing fructosamines, preventing irreversible advanced glycation end-products (AGEs). Recent high-resolution structures of FN3K by <span><span>Garg and On <em>et al</em>.</span><svg><path></path></svg></span> reveal key active-site features, highlighting unique regulatory mechanisms and potential druggable sites and providing a foundation for structure-guided drug development against this target.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 372-373"},"PeriodicalIF":11.6000,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"FN3K: the (un)sweetest kinase\",\"authors\":\"Joyce Ogidigo , Reena Kumari , Viraj R. Sanghvi\",\"doi\":\"10.1016/j.tibs.2025.03.009\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Fructosamine 3-kinase (FN3K) mitigates excessive protein glycation by phosphorylating and destabilizing fructosamines, preventing irreversible advanced glycation end-products (AGEs). Recent high-resolution structures of FN3K by <span><span>Garg and On <em>et al</em>.</span><svg><path></path></svg></span> reveal key active-site features, highlighting unique regulatory mechanisms and potential druggable sites and providing a foundation for structure-guided drug development against this target.</div></div>\",\"PeriodicalId\":440,\"journal\":{\"name\":\"Trends in Biochemical Sciences\",\"volume\":\"50 5\",\"pages\":\"Pages 372-373\"},\"PeriodicalIF\":11.6000,\"publicationDate\":\"2025-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Trends in Biochemical Sciences\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0968000425000581\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Trends in Biochemical Sciences","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0968000425000581","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
果糖胺 3 激酶(FN3K)通过磷酸化和破坏果糖胺的稳定性,防止不可逆转的高级糖化终产物(AGEs),从而减轻蛋白质的过度糖化。Garg 和 On 等人最近对 FN3K 的高分辨率结构进行了研究,揭示了关键的活性位点特征,突出了独特的调控机制和潜在的可用药位点,为针对这一靶点的结构引导药物开发奠定了基础。
Fructosamine 3-kinase (FN3K) mitigates excessive protein glycation by phosphorylating and destabilizing fructosamines, preventing irreversible advanced glycation end-products (AGEs). Recent high-resolution structures of FN3K by Garg and On et al. reveal key active-site features, highlighting unique regulatory mechanisms and potential druggable sites and providing a foundation for structure-guided drug development against this target.
期刊介绍:
For over 40 years, Trends in Biochemical Sciences (TIBS) has been a leading publication keeping readers informed about recent advances in all areas of biochemistry and molecular biology. Through monthly, peer-reviewed issues, TIBS covers a wide range of topics, from traditional subjects like protein structure and function to emerging areas in signaling and metabolism. Articles are curated by the Editor and authored by top researchers in their fields, with a focus on moving beyond simple literature summaries to providing novel insights and perspectives. Each issue primarily features concise and timely Reviews and Opinions, supplemented by shorter articles including Spotlights, Forums, and Technology of the Month, as well as impactful pieces like Science & Society and Scientific Life articles.