Open AccessA Common Structural Component for �-Subunit Mediated Modulation of Slow Inactivation in Different KVChannels
Author(s) -
Nathalie StrutzSeebohm,
Ulrike Henrion,
Nicole Schmitt,
Eric SchulzeBahr,
Guiscard Seebohm
Publication year - 2013
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000350115
Subject(s) - chemistry , kcsa potassium channel , potassium channel , biophysics , protein subunit , mutagenesis , ion channel , amino acid , gating , kinetics , binding site , alanine , biochemistry , stereochemistry , mutation , biology , receptor , physics , quantum mechanics , gene
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.
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