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Solution structure and dynamics of mouse ARMET
Author(s) -
Hoseki Jun,
Sasakawa Hiroaki,
Yamaguchi Yoshiki,
Maeda Momoe,
Kubota Hiroshi,
Kato Koichi,
Nagata Kazuhiro
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.03.008
Subject(s) - endoplasmic reticulum , linker , biophysics , chemistry , trypsin , molecule , relaxation (psychology) , unfolded protein response , crystallography , biochemistry , biology , enzyme , computer science , organic chemistry , neuroscience , operating system
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 α‐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 15 N 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.