{"title":"How protein disorder turns internal dynamics into a long-range regulatory switch","authors":"","doi":"10.1038/s41594-025-01588-4","DOIUrl":null,"url":null,"abstract":"Understanding how proteins are regulated remains a fundamental challenge in molecular biology. Our findings demonstrate how a flexible, disordered protein segment — an intrinsically disordered region — can remotely silence or activate protein function by tuning internal dynamics via an entropy-driven regulatory mechanism without structural change or direct protein contact.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"103 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-06-16","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/s41594-025-01588-4","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Understanding how proteins are regulated remains a fundamental challenge in molecular biology. Our findings demonstrate how a flexible, disordered protein segment — an intrinsically disordered region — can remotely silence or activate protein function by tuning internal dynamics via an entropy-driven regulatory mechanism without structural change or direct protein contact.