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Charybdotoxin and Margatoxin Acting on the Human Voltage-Gated Potassium Channel hKv1.3 and Its H399N Mutant. An Experimental and Computational Comparison
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SYSNO ASEP 0382088 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Charybdotoxin and Margatoxin Acting on the Human Voltage-Gated Potassium Channel hKv1.3 and Its H399N Mutant. An Experimental and Computational Comparison Author(s) Nikouee, A. (DE)
Khabiri, Morteza (UEK-B) SAI, ORCID
Grissmer, S. (DE)
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAINumber of authors 4 Source Title Journal of Physical Chemistry B. - : American Chemical Society - ISSN 1520-6106
Roč. 116, č. 17 (2012), s. 5132-5140Number of pages 9 s. Language eng - English Country US - United States Keywords Charbydotoxin ; dependent k + channel ; constant-pressure ; molecular dynamics simulations ; scorpion toxin ; force-field Subject RIV CE - Biochemistry Institutional support RVO:67179843 - RVO:67179843 UT WOS 000303426400004 DOI https://doi.org/10.1021/jp2102463 Annotation The effect of the pore-blocking peptides charybdotoxin and margatoxin, both scorpion toxins, on currents through human voltage-gated hK(v)1.3 wild-type and hK(v)1.3_H399N mutant potassium channels was characterized by the whole-cell patch clamp technique. In the mutant channels, both toxins hardly blocked current through the channels, although they did prevent C-type inactivation by slowing down the current decay during depolarization. Molecular dynamics simulations suggested that the fast current decay in the mutant channel was a consequence of amino acid reorientations behind the selectivity filter and indicated that the rigidity-flexibility in that region played a key role in its interactions with scorpion toxins. A channel with a slightly more flexible selectivity filter region exhibits distinct interactions with scorpion toxins. Our studies suggest that the toxin-channel interactions might partially restore rigidity in the selectivity filter and thereby prevent the structural rearrangements associated with C-type inactivation. Workplace Global Change Research Institute Contact Nikola Šviková, svikova.n@czechglobe.cz, Tel.: 511 192 268 Year of Publishing 2013
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