2RQY

Solution structure and dynamics of mouse ARMET

Summary for 2RQY

• Entry DOI: 10.2210/pdb2rqy/pdb
• Descriptor: Putative uncharacterized protein (1 entity in total)
• Functional Keywords: endoplasmic reticulum, unfolded protein response, cxxc motif, unknown function
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 19926.19

Authors

Hoseki, J.,Sasakawa, H.,Yamaguchi, Y.,Maeda, M.,Kubota, H.,Kato, K.,Nagata, K. (deposition date: 2010-01-26, release date: 2010-04-21, Last modification date: 2024-11-06)

Primary citation

Hoseki, J.,Sasakawa, H.,Yamaguchi, Y.,Maeda, M.,Kubota, H.,Kato, K.,Nagata, K.
Solution structure and dynamics of mouse ARMET.
Febs Lett., 584:1536-1542, 2010

PubMed Abstract: 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.

PubMed: 20214902
DOI: 10.1016/j.febslet.2010.03.008

Experimental method

SOLUTION NMR