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The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.  相似文献   
2.
The structure of the cytoplasmic assembly of voltage-dependent K+ channels was solved by x-ray crystallography at 2.1 angstrom resolution. The assembly includes the cytoplasmic (T1) domain of the integral membrane alpha subunit together with the oxidoreductase beta subunit in a fourfold symmetric T1(4)beta4 complex. An electrophysiological assay showed that this complex is oriented with four T1 domains facing the transmembrane pore and four beta subunits facing the cytoplasm. The transmembrane pore communicates with the cytoplasm through lateral, negatively charged openings above the T1(4)beta4 complex. The inactivation peptides of voltage-dependent K(+) channels reach their site of action by entering these openings.  相似文献   
3.
Jørgensen  L. N.  Matzen  N.  Heick  T. M.  Havis  N.  Holdgate  S.  Clark  B.  Blake  J.  Glazek  M.  Korbas  M.  Danielewicz  J.  Maumene  C.  Rodemann  B.  Weigand  S.  Kildea  S.  Bataille  C.  Brauna-Morževska  E.  Gulbis  K.  Ban  R.  Berg  G.  Semaskiene  R.  Stammler  G. 《植物病害和植物保护杂志》2021,128(1):287-301
Journal of Plant Diseases and Protection - Septoria tritici blotch (STB; Zymoseptoria tritici) is the most important leaf disease of wheat in Northern and Western Europe. The problem of fungicide...  相似文献   
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