ИСТИНА

Voltage-gated potassium (K+) channels are transmembrane pore proteins and contribute to the regulation of membrane potential and, consequently, to cell excitability. Kv1.2 channels play pivotal role in maintaining of resting membrane potential and, consequently, regulation of cellular excitability of neurons. Their blockers have a high importance not only as probes the fundamental channel functioning investigation, but also as a potential drug for treatment epilepsy [1]. Goal of the current study was an interface analysis in complexes of Kv1.2 channel with peptide toxins MeuKTx1, MeuKTx3 и MeuKTx3B, derived from M. eupeus venom.