期刊
FEBS LETTERS
卷 584, 期 8, 页码 1536-1542出版社
WILEY
DOI: 10.1016/j.febslet.2010.03.008
关键词
ER stress; Solution structure; Positive charge; Domain movement
资金
- Grants-in-Aid for Creative Scientific Research [19GS0314]
- Scientific Research [19058008, 21370050]
- The Takeda Foundation
- Grants-in-Aid for Scientific Research on Priority Areas [20059030]
- Scientific Research on Innovative Areas [20107004]
- Ministry of Education, Culture, Sports, Science and Technology
- Grants-in-Aid for Scientific Research [19058008, 20059030, 19GS0314] Funding Source: KAKEN
ARMET is an endoplasmic reticulum (ER) stress-inducible protein that is required for maintaining cell viability under ER stress conditions. However, the exact molecular mechanisms by which ARMET protects cells are unknown. Here, we have analyzed the solution structure of ARMET. ARMET has an entirely alpha-helical structure, which is composed of two distinct domains. Positive charges are dispersed on the surfaces of both domains and across a linker structure. Trypsin digestion and N-15 relaxation experiments indicate that the tumbling of the N-terminal and C-terminal domains is effectively independent. These results suggest that ARMET may hold a negatively charged molecule using the two positively charged domains. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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