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Toxins 2014, 6(7), 2149-2161;

Binding Modes of Two Scorpion Toxins to the Voltage-Gated Potassium Channel Kv1.3 Revealed from Molecular Dynamics

Research School of Biology, Australian National University, Canberra, ACT 0200, Australia
Author to whom correspondence should be addressed.
Received: 30 May 2014 / Revised: 8 July 2014 / Accepted: 10 July 2014 / Published: 22 July 2014
(This article belongs to the Special Issue Ion Channel Neurotoxins)
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Molecular dynamics (MD) simulations are used to examine the binding modes of two scorpion toxins, margatoxin (MgTx) and hongotoxin (HgTx), to the voltage gated K+ channel, Kv1.3. Using steered MD simulations, we insert either Lys28 or Lys35 of the toxins into the selectivity filter of the channel. The MgTx-Kv1.3 complex is stable when the side chain of Lys35 from the toxin occludes the channel filter, suggesting that Lys35 is the pore-blocking residue for Kv1.3. In this complex, Lys28 of the toxin forms one additional salt bridge with Asp449 just outside the filter of the channel. On the other hand, HgTx forms a stable complex with Kv1.3 when the side chain of Lys28 but not Lys35 protrudes into the filter of the channel. A survey of all the possible favorable binding modes of HgTx-Kv1.3 is carried out by rotating the toxin at 3° intervals around the channel axis while the position of HgTx-Lys28 relative to the filter is maintained. We identify two possible favorable binding modes: HgTx-Arg24 can interact with either Asp433 or Glu420 on the vestibular wall of the channel. The dissociation constants calculated from the two binding modes of HgTx-Kv1.3 differ by approximately 20 fold, suggesting that the two modes are of similar energetics. View Full-Text
Keywords: margatoxin; hongotoxin; Kv1.3; molecular dynamics; scorpion toxins margatoxin; hongotoxin; Kv1.3; molecular dynamics; scorpion toxins

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Chen, R.; Chung, S.-H. Binding Modes of Two Scorpion Toxins to the Voltage-Gated Potassium Channel Kv1.3 Revealed from Molecular Dynamics. Toxins 2014, 6, 2149-2161.

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