Journal
BIOPHYSICAL JOURNAL
Volume 91, Issue 11, Pages L90-L92Publisher
BIOPHYSICAL SOCIETY
DOI: 10.1529/biophysj.106.096065
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Funding
- NCRR NIH HHS [R01 RR014812, RR-14812] Funding Source: Medline
- NIGMS NIH HHS [GM-74637, R01 GM068002, GM-68002, R01 GM074637] Funding Source: Medline
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Voltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close in response to changes in transmembrane potential. Recent experimental studies suggest that VS domains are independent structural units. This independence is revealed dramatically by a voltage-dependent proton-selective channel (Hv), which has a sequence homologous to the VS domains of voltage-gated potassium channels (Kv). Here we show by means of molecular dynamics simulations that the isolated open-state VS domain of the KvAP channel in a lipid membrane has a configuration consistent with a water channel, which we propose as a common feature underlying the conductance of protons, and perhaps other cations, through VS domains.
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