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Abstract
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 α subunit together with the oxidoreductase β subunit in a fourfold symmetric T14β4 complex. An electrophysiological assay showed that this complex is oriented with four T1 domains facing the transmembrane pore and four β subunits facing the cytoplasm. The transmembrane pore communicates with the cytoplasm through lateral, negatively charged openings above the T14β4complex. The inactivation peptides of voltage-dependent K+channels reach their site of action by entering these openings.
