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DOI | 10.1126/science.aax1280 |
Structural basis for client recognition and activity of Hsp40 chaperones | |
Jiang, Yajun; Rossi, Paolo; Kalodimos, Charalampos G. | |
2019-09-20 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2019 |
卷号 | 365期号:6459页码:1313-+ |
文章类型 | Article |
语种 | 英语 |
国家 | USA |
英文摘要 | Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000487547400049 |
WOS关键词 | CRYSTAL-STRUCTURE ; CO-CHAPERONES ; YEAST HSP40 ; J-PROTEINS ; HSP70 ; NMR ; BINDING ; DNAK ; DOMAIN ; CRYSTALLOGRAPHY |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/202352 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | St Jude Childrens Res Hosp, Dept Struct Biol, 332 N Lauderdale St, Memphis, TN 38105 USA |
推荐引用方式 GB/T 7714 | Jiang, Yajun,Rossi, Paolo,Kalodimos, Charalampos G.. Structural basis for client recognition and activity of Hsp40 chaperones[J]. SCIENCE,2019,365(6459):1313-+. |
APA | Jiang, Yajun,Rossi, Paolo,&Kalodimos, Charalampos G..(2019).Structural basis for client recognition and activity of Hsp40 chaperones.SCIENCE,365(6459),1313-+. |
MLA | Jiang, Yajun,et al."Structural basis for client recognition and activity of Hsp40 chaperones".SCIENCE 365.6459(2019):1313-+. |
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