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Exploring the Viral Channel Kcv_PBCV-1 Function via Computation.

Alma E V Andersson¹, Marina A Kasimova¹, Lucie Delemotte²

¹Science for Life Laboratory, Department of Applied Physics, KTH Royal Institute of Technology, Box 1031, SE-171 21, Solna, Sweden.

The Journal of Membrane Biology

|February 25, 2018

Summary

Viral potassium channels (Kcv) offer insights into ion conduction. Simulations reveal fast gating mechanisms involving filter carbonyl re-orientation and ion relocation, with lipid interactions also observed.

Keywords:

Conduction Gating Homology modeling Molecular dynamics simulations Protein–lipid interaction Viral ion channel

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Area of Science:

Structural biology
Biophysics
Molecular biology

Background:

Viral potassium channels (Kcv) share structural homology with cellular potassium-selective ion channels.
Their simpler structure makes them valuable for studying ion conduction and channel gating principles.

Purpose of the Study:

To develop a homology model of the open state of viral potassium channels.
To investigate the mechanisms of potassium ion conduction and channel gating.
To explore the interaction of viral potassium channels with lipid bilayers.

Main Methods:

Homology modeling of the viral potassium channel open state.
Validation through blocker binding studies and ion conduction monitoring.
Molecular dynamics simulations to analyze ion transport and channel gating.

Main Results:

A validated homology model of the viral potassium channel open state was generated.
Simulations suggest fast gating involves re-orientation of selectivity filter carbonyl groups during ion transport.
Voltage sensitivity may arise from potassium ion relocation within the selectivity filter.
Lipid binding was observed in the inter-subunit region of the channel.

Conclusions:

The study provides a model for viral potassium channels, elucidating potential fast gating mechanisms.
Ion relocation within the selectivity filter contributes to voltage sensitivity.
Lipid interactions play a role in channel structure and function.
The provided model facilitates further research into viral potassium channel structure-function relationships.