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Toxins 2017, 9(11), 354;

Molecular Dynamics Simulation Reveals Specific Interaction Sites between Scorpion Toxins and Kv1.2 Channel: Implications for Design of Highly Selective Drugs

Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China
College of Resources and Environment, University of Chinese Academy of Sciences, Beijing 100049, China
Author to whom correspondence should be addressed.
Academic Editors: Bryan Grieg Fry and Steve Peigneur
Received: 29 August 2017 / Revised: 15 October 2017 / Accepted: 19 October 2017 / Published: 1 November 2017
(This article belongs to the Special Issue Toxins in Drug Discovery and Pharmacology)
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The Kv1.2 channel plays an important role in the maintenance of resting membrane potential and the regulation of the cellular excitability of neurons, whose silencing or mutations can elicit neuropathic pain or neurological diseases (e.g., epilepsy and ataxia). Scorpion venom contains a variety of peptide toxins targeting the pore region of this channel. Despite a large amount of structural and functional data currently available, their detailed interaction modes are poorly understood. In this work, we choose four Kv1.2-targeted scorpion toxins (Margatoxin, Agitoxin-2, OsK-1, and Mesomartoxin) to construct their complexes with Kv1.2 based on the experimental structure of ChTx-Kv1.2. Molecular dynamics simulation of these complexes lead to the identification of hydrophobic patches, hydrogen-bonds, and salt bridges as three essential forces mediating the interactions between this channel and the toxins, in which four Kv1.2-specific interacting amino acids (D353, Q358, V381, and T383) are identified for the first time. This discovery might help design highly selective Kv1.2-channel inhibitors by altering amino acids of these toxins binding to the four channel residues. Finally, our results provide new evidence in favor of an induced fit model between scorpion toxins and K+ channel interactions. View Full-Text
Keywords: Kv1.2 channel; scorpion toxin; molecular dynamics simulation Kv1.2 channel; scorpion toxin; molecular dynamics simulation

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Yuan, S.; Gao, B.; Zhu, S. Molecular Dynamics Simulation Reveals Specific Interaction Sites between Scorpion Toxins and Kv1.2 Channel: Implications for Design of Highly Selective Drugs. Toxins 2017, 9, 354.

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