Abstract
Expressed primarily in cardiac myocytes, the hERG channel (Kv11.1) is a voltage-gated potassium channel that facilitates a repolarizing K+ current during the cardiac action potential (CAP). In response to changes in membrane potential, the hERG channel undergoes transitions from closed to open and inactivated states. Utilizing atomistic molecular modeling and docking simulations, we aim to assess the state-specific binding of drugs to the hERG channel utilizing structural models of open and inactivated hERG channels.
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