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A voltage-sensor water pore.

J Alfredo Freites1, Douglas J Tobias, Stephen H White

  • 1Institute for Genomics and Bioinformatics, University of California, Irvine, CA 92697, USA.

Biophysical Journal
|October 3, 2006
PubMed
Summary
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Voltage-sensor (VS) domains act as independent units in ion channels. Molecular dynamics simulations reveal the VS domain of KvAP channels forms a water channel, potentially explaining proton conductance.

Area of Science:

  • Molecular Biophysics
  • Ion Channel Physiology
  • Structural Biology

Background:

  • Voltage-sensor (VS) domains regulate the opening and closing of voltage-gated ion channels based on transmembrane potential.
  • Experimental evidence suggests VS domains function as independent structural units.
  • A voltage-dependent proton channel (Hv) shares sequence homology with VS domains of potassium channels (Kv).

Purpose of the Study:

  • To investigate the structural configuration of an isolated voltage-sensor domain.
  • To explore the potential role of the VS domain in ion conductance.
  • To determine if the VS domain itself can form a conductive pathway.

Main Methods:

  • Molecular dynamics (MD) simulations were employed.
  • The open-state VS domain of the KvAP channel was simulated in a lipid membrane environment.

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Main Results:

  • The isolated, open-state VS domain of the KvAP channel adopted a configuration resembling a water channel.
  • This water channel structure was observed within a lipid membrane.
  • The simulated structure suggests a mechanism for ion passage through VS domains.

Conclusions:

  • The VS domain of the KvAP channel, when isolated, can form a water-filled channel structure.
  • This finding supports the hypothesis that VS domains are independent functional units.
  • The proposed water channel may represent a common mechanism for proton and potentially other cation conductance through VS domains.