Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure and dynamics of mouse ARMET.,Hoseki J, Sasakawa H, Yamaguchi Y, Maeda M, Kubota H, Kato K, Nagata K FEBS Lett. 2010 Apr 16;584(8):1536-42. Epub 2010 Mar 6. PMID:20214902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoseki J, Sasakawa H, Yamaguchi Y, Maeda M, Kubota H, Kato K, Nagata K. Solution structure and dynamics of mouse ARMET. FEBS Lett. 2010 Apr 16;584(8):1536-42. Epub 2010 Mar 6. PMID:20214902 doi:10.1016/j.febslet.2010.03.008
