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Solution structure and dynamics of mouse ARMET.
Hoseki, Jun; Sasakawa, Hiroaki; Yamaguchi, Yoshiki; Maeda, Momoe; Kubota, Hiroshi; Kato, Koichi; Nagata, Kazuhiro.
Afiliação
  • Hoseki J; Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
FEBS Lett ; 584(8): 1536-42, 2010 Apr 16.
Article em En | MEDLINE | ID: mdl-20214902
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.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Ressonância Magnética Nuclear Biomolecular Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2010 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Ressonância Magnética Nuclear Biomolecular Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2010 Tipo de documento: Article