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Kv channel S6 helix as a molecular switch: simulation studies.

J N Bright¹, M S P Sansom

¹Research School of Chemistry, The Australian National University, Canberra, Australia.

IEE Proceedings. Nanobiotechnology

|February 16, 2006

Summary

The PVP motif in voltage-gated potassium (Kv) channels acts as a molecular hinge, facilitating channel gating. This finding reveals a complex nanoswitch mechanism involving S6 helix flexibility.

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Area of Science:

Biophysics
Molecular Biology
Structural Biology

Background:

Ion channels are crucial for cell physiology, with most possessing a gating mechanism.
Voltage-gated potassium (Kv) channels are essential, and their gating involves the S6 helix.

Purpose of the Study:

To investigate the role of the conserved PVP sequence motif in the S6 helix of Kv channels.
To explore the conformational dynamics of the S6 helix hinge using molecular dynamics simulations.

Main Methods:

Molecular dynamics simulations of Kv channel fragments (monomer and tetramer models).
Simulations were conducted using membrane mimetic (octane slab).
Comparison with crystal structures of Kv channels, including KvAP.

Main Results:

The PVP motif functions as a molecular hinge in the S6 helix.
S6 helix flexibility is modulated by the protein but remains significant.
Simulation results support a gating model involving S6 helix bending at the PVP motif and a glycine residue.

Conclusions:

Kv channel gating involves a complex nanoswitch mechanism.
The S6 helix, with its PVP motif and adjacent glycine, acts as a key component of this nanoswitch.
The gating mechanism relies on three rigid helical sections connected by two molecular hinges.

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