The K+ channel encoded by the human ether-a-go-go related gene (HERG) is on
e of many ion channels that are crucial for normal action potential repolar
ization in cardiac myocytes, HERG encodes the pore-forming subunit of the r
apid component of the delayed rectifier K+ channel, I-K(Vr). HERG K+ channe
ls are of considerable pharmaceutical interest as possible therapeutic targ
ets for anti-arrhythmic agents and as the molecular target responsible for
the cardiac toxicity of a wide range of pharmaceutical agents. Recent studi
es of the molecular basis of the promiscuity of HERG K+ channel drug bindin
g has not only started to shed light on this tricky pharmaceutical problem
but has also provided further insights into the structure and function of H
ERG K+ channels.