Solution structure and dynamics of mouse ARMET.
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 (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.
Hoseki
Jun
J
Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
Sasakawa
Hiroaki
H
Yamaguchi
Yoshiki
Y
Maeda
Momoe
M
Kubota
Hiroshi
H
Kato
Koichi
K
Nagata
Kazuhiro
K
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009414:Nerve Growth Factors; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012996:Solutions
C534671:MANF protein, mouse; D009414:Nerve Growth Factors; D011506:Proteins; D012996:Solutions