Interfacial gating triad is crucial for electromechanical transduction in voltage-activated potassium channels.

ABSTRACT: Voltage-dependent potassium channels play a crucial role in electrical excitability and cellular signaling by regulating potassium ion flux across membranes. Movement of charged residues in the voltage-sensing domain leads to a series of conformational changes that culminate in channel opening in response to changes in membrane potential. However, the molecular machinery that relays these conformational changes from voltage sensor to the pore is not well understood. Here we use generalized interaction-energy analysis (GIA) to estimate the strength of site-specific interactions between amino acid residues putatively involved in the electromechanical coupling of the voltage sensor and pore in the outwardly rectifying KV channel. We identified candidate interactors at the interface between th

SUBMITTER: Chowdhury S 

PROVIDER: S-EPMC4210428 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature