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Biophys. J. BioFAST: First Published July 13, 2007. doi:10.1529/biophysj.107.114561
© 2007 by the Biophysical Society.

A more recent version of this article appeared on September 15, 2007.
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CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

The S631A mutation causes a mechanistic switch in the block of hERG channels by CnErg1

Adam P Hill 1, Terry J Campbell 2, Paramjit S Bansal 3, Philip W Kuchel 3 and Jamie Vandenberg 4*

1 VCCRI
2 University of New South Wales
3 University of Sydney
4 Victor Chang

* To whom correspondence should be addressed. E-mail: j.vandenberg{at}victorchang.unsw.edu.au.

Submitted on June 8, 2007
Revised on June 21, 2007
Accepted on 26 June 2007


  Abstract
We have studied the interaction CnErg1, a member of the {gamma}-KTX subfamily of scorpion toxins with the inactivation deficient S631A hERG channel. In the background of this mutation we observed a mechanistic switch from 'turret' block, characteristic of the action of {gamma}-KTXs on Kv11-type channels, to 'pore plugging', characteristic of {alpha}-KTX block of Kv1-type channels. We suggest this reflects destabilization of the outer pore (turret region) of hERG allowing access of the toxin molecule to directly plug the conduction pathway.

Key Words: hERG, inactivation, ion channel, potassium channel, structure, toxin






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Copyright © 2007 by the Biophysical Society.