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The structure of the potassium channel: molecular basis of K+ conduction and selectivity.
TLDR
The architecture of the pore establishes the physical principles underlying selective K+ conduction, which promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. Expand
Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution
TLDR
Here it is shown how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entry way. Expand
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
TLDR
This work presents the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 Å, respectively, and establishes the physical and chemical basis of their anion selectivity. Expand
Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K+ Channel
TLDR
Electrostatic properties of the side portals and positions of the T1 domain and β sub unit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the β subunit. Expand
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
TLDR
The detailed structure of a chimaeric voltage-dependent K+ channel, which the authors call the ‘paddle-chimaera channel’, is described, which explains charge stabilization within the membrane and suggests a mechanism for voltage-sensor movements and pore gating. Expand
X-ray structure of a voltage-dependent K+ channel
TLDR
The structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix, is presented and a crystal structure of the full-length channel at a resolution of 3.2 Å is determined, which suggests that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane. Expand
Crystal structure and mechanism of a calcium-gated potassium channel
TLDR
This work has cloned, expressed, analysed electrical properties, and determined the crystal structure of a K+ channel (MthK) from Methanobacterium thermoautotrophicum in the Ca2+-bound, opened state. Expand
Crystal Structures of a Complexed and Peptide-Free Membrane Protein–Binding Domain: Molecular Basis of Peptide Recognition by PDZ
TLDR
X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined and reveal that specific side chain interactions and a prominent hydrophobic pocket explain the selective recognition of the C-terminal consensus sequence. Expand
The open pore conformation of potassium channels
TLDR
Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K+ channels, both ligand- and voltage-gated. Expand
Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling
TLDR
The x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing the investigation of the mechanism by which these channels sense cell membrane voltage. Expand
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