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2021 - Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization

 icon sp96   SyncroPatch 384PE (a predecessor model of the SyncroPatch 384 instrument) publication in BMC Molecular and Cell Biology (2021)

Authors:
Matsumura K., Shimomura T., Kubo Y., Oka T., Kobayashi N., Imai S., Yanase N., Akimoto M., Fukuda M., Yokogawa M., Ikeda K., Kurita J., Nishimura Y., Shimada I., Osawa M.

Journal:

BMC Molecular and Cell Biology 22, 3 (2021) doi: 10.1186/s12860-020-00337-3


Abstract: 

Human ether-à-go-go-related gene potassium channel 1 (hERG) is a voltage-gated potassium channel, the voltage-sensing domain (VSD) of which is targeted by a gating-modifier toxin, APETx1. APETx1 is a 42-residue peptide toxin of sea anemone Anthopleura elegantissima and inhibits hERG by stabilizing the resting state. A previous study that conducted cysteine-scanning analysis of hERG identified two residues in the S3-S4 region of the VSD that play important roles in hERG inhibition by APETx1. However, mutational analysis of APETx1 could not be conducted as only natural resources have been available until now. Therefore, it remains unclear where and how APETx1 interacts with the VSD in the resting state.


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