Gulbis J M, Zhou M, Mann S, MacKinnon R
Howard Hughes Medical Institute and Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Science. 2000 Jul 7;289(5476):123-7. doi: 10.1126/science.289.5476.123.
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.
电压依赖性钾通道的胞质组件结构通过X射线晶体学在2.1埃分辨率下得以解析。该组件包括完整膜α亚基的胞质(T1)结构域以及氧化还原酶β亚基,形成一个四重对称的T1(4)β4复合体。电生理分析表明,该复合体的取向是四个T1结构域面向跨膜孔,四个β亚基面向细胞质。跨膜孔通过T1(4)β4复合体上方横向的带负电荷开口与细胞质相通。电压依赖性钾通道的失活肽通过进入这些开口到达其作用位点。