Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
FEBS Lett. 2010 Apr 16;584(8):1536-42. doi: 10.1016/j.febslet.2010.03.008. Epub 2010 Mar 6.
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.
ARMEt 是内质网(ER)应激诱导蛋白,在 ER 应激条件下维持细胞活力是必需的。然而,ARMEt 保护细胞的确切分子机制尚不清楚。在这里,我们分析了 ARMEt 的溶液结构。ARMEt 具有完全的α-螺旋结构,由两个不同的结构域组成。正电荷分散在两个结构域的表面和连接结构上。胰蛋白酶消化和(15)N 弛豫实验表明,N 端和 C 端结构域的翻滚是有效的独立的。这些结果表明,ARMEt 可能使用两个正电荷结构域来结合带负电荷的分子。