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Mar. Drugs 2006, 4(3), 143-156; doi:10.3390/md403143
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The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels

1,2 and 1,*
1 Department of Biology, Utah State University, 5305 Old Main Hill, Logan, Utah, 84322-5305, USA 2 Present address: Department of Molecular and Cellular Physiology, Stanford University, 279 Campus Drive, Beckman Center B115, Stanford, California, 94305, USA
* Author to whom correspondence should be addressed.
Received: 22 November 2005 / Accepted: 24 February 2006 / Published: 6 April 2006
(This article belongs to the Special Issue Marine Drugs and Ion Channels)
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Abstract

Tetrodotoxin (TTX) is a highly specific blocker of voltage-gated sodium channels. The dissociation constant of block varies with different channel isoforms. Until recently, channel resistance was thought to be primarily imparted by amino acid substitutions at a single position in domain I. Recent work reveals a novel site for tetrodotoxin resistance in the P-region of domain IV.
Keywords: neurotoxin; TTX; NaV; inward sodium current; voltage clamp neurotoxin; TTX; NaV; inward sodium current; voltage clamp
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Geffeney, S.L.; Ruben, C. The Structural Basis and Functional Consequences of Interactions Between Tetrodotoxin and Voltage-Gated Sodium Channels. Mar. Drugs 2006, 4, 143-156.

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