Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.

ABSTRACT: Voltage-dependent potassium (K_v) channels play a fundamental role in neuronal and cardiac excitability and are potential therapeutic targets. They assemble as tetramers with a centrally located pore domain surrounded by a voltage-sensing domain (VSD), which is critical for sensing transmembrane potential and subsequent gating. Although the sensor is supposed to be in "Up" conformation in both n-octylglucoside (OG) micelles and phospholipid membranes in the absence of membrane potential, toxins that bind VSD and modulate the gating behavior of K_v channels exhibit dramatic affinity differences in these membrane-mimetic systems. In this study, we have monitored the structural dynamics of the S3b-S4 loop of the paddle motif in activated conformation of KvAP-VSD by site-di

SUBMITTER: Das A 

PROVIDER: S-EPMC7036696 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature