Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 116, Issue 17, Pages 5132-5140Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp2102463
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Funding
- Czech Science Foundation [203/08/0114]
- Academy of Sciences of the Czech Republic
- DFG [Gr 848/14-1]
- University of South Bohemia [GAJU 170/2010/P]
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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.
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