Journal
BIOPHYSICAL JOURNAL
Volume 93, Issue 6, Pages L32-L34Publisher
BIOPHYSICAL SOC
DOI: 10.1529/biophysj.107.114561
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We have studied the interaction of 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.
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