Structure of the Cytoplasmic β Subunit--T1 Assembly of Voltage-Dependent K + Channels
- 7 July 2000
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 289 (5476) , 123-127
- https://doi.org/10.1126/science.289.5476.123
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.Keywords
This publication has 29 references indexed in Scilit:
- Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channelJournal of Molecular Biology, 1999
- The Structure of the Potassium Channel: Molecular Basis of K + Conduction and SelectivityScience, 1998
- Potassium Channel ä and β Subunits Assemble in the Endoplasmic ReticulumPublished by Elsevier ,1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Selective Interaction of Voltage-gated K+ Channel β-Subunits with α-SubunitsJournal of Biological Chemistry, 1996
- Revealing the Architecture of a K + Channel Pore Through Mutant Cycles with a Peptide InhibitorScience, 1995
- A conductance maximum observed in an inward-rectifier potassium channel.The Journal of general physiology, 1994
- Inactivation properties of voltage-gated K+ channels altered by presence of β-subunitNature, 1994
- The inactivation gate of the Shaker K+ channel behaves like an open-channel blockerNeuron, 1991
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988