期刊
MOLECULAR CELL
卷 39, 期 2, 页码 269-281出版社
CELL PRESS
DOI: 10.1016/j.molcel.2010.05.010
关键词
-
资金
- KAKENHI [19678001, 21870044]
- Riken special postdoctoral research fellowship
- Wellcome Trust [080041/Z/06/Z]
- Wellcome Trust [080041/Z/06/Z] Funding Source: Wellcome Trust
- Grants-in-Aid for Scientific Research [21870044] Funding Source: KAKEN
Hsp90-mediated function of NLR receptors in plant and animal innate immunity depends on the cochaperone Sgt1 and, at least in plants, on a cysteine- and histidine-rich domains (CHORD)-containing protein Rar1. Functionally, CHORD domains are associated with CS domains, either within the same protein, as in the mammalian melusin and Chp1,or in separate but interacting proteins, as in the plant Ran l and Sgt1. Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90. We have now determined the structure of an Hsp90-CS-CHORD ternary complex, providing a framework for understanding the dynamic nature of Hsp90-Rar1-Sgt1 complexes. Mutational and biochemical analyses define the architecture of the ternary complex that recruits nucleotide-binding leucine-rich repeat receptors (NLRs) by manipulating the structural elements to control the ATPase-dependent conformational cycle of the chaperone.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据