Abstract
The voltage-sensing domain (VSD) is a 4-helix transmembrane (TM) regulatory domain that undergoes a conformational change in response to a change in TM potential. While originally identified in voltage-gated cation channels, the VSD has since been observed in voltage-gated proton channels and voltage-sensing lipid phosphatases. Therefore, sensitivity to a change in TM potential appears to rely on an evolutionarily unique and structurally conserved domain. Moreover, VSDs have been fine-tuned by evolution to sense a wide range of polarization states. Here, we develop a robust hidden Markov model (HMM) of the VSD sequence for the purpose of detecting and aligning remote homologues. Then, we use statistical coupling analysis and molecular dynamics simulations to correlate highly-conserved residues and residue pairs with the atomic-level details of VSD structure, function, and tunability.
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