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Potassium channels are tetrameric proteins providing potassium selective passage through lipid embedded proteinaceous pores with highest fidelity. The selectivity results from binding to discrete potassium binding sites and stabilization of a hydrated potassium ion in a central internal cavity. The four potassium binding sites, generated by the conserved TTxGYGD signature sequence are formed by the backbone carbonyls of the amino acids TXGYG. Residues KV1.5-Val481, KV4.3-Leu368 and KV7.1- Ile 313 represent the amino acids in the X position of the respective channels.

A Common Structural Component for �-Subunit Mediated Modulation of Slow Inactivation in Different KVChannels

A Common Structural Component for �-Subunit Mediated Modulation of Slow Inactivation in Different K_VChannels