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A model of the selectivity filter of a voltage-gated K+ (Kv) channel formed by an eight-stranded beta-barrel is compared with physiological properties of the channel. Continuum electrostatic calculations suggest that only two of the eight Asp sidechains at the extracellular mouth of the pore will ionise. A ring of four Tyr sidechains forms the narrowest region of the pore. Molecular dynamic simulations of the potential energy of a K+ ion as translated along the model pore indicate that the two ionised Asp sidechains and the hydroxyl groups of the Tyr sidechains stabilise the partially desolvated ion as it passes through the narrowest region.


Journal article


Biochim Biophys Acta

Publication Date





1 - 7


Amino Acid Sequence, Animals, Computer Simulation, Ion Transport, Models, Molecular, Molecular Sequence Data, Potassium Channels, Protein Structure, Tertiary, Proteins, Structure-Activity Relationship, Thermodynamics, Water