Key result
Replacing Trp207 in human HV1 with Ala, Ser, or Phe accelerated channel opening by 100-fold and decreased activation energy from 30-38 kcal/mol to 22 kcal/mol, indicating Trp207 favors a closed state.
Population
Human voltage-gated proton channel and analogous channels from Karlodinium veneficum and Emiliania huxleyi
Comparison
Mutation of Trp207 to Ala, Ser, or Phe vs Wild-type (WT) channels
Design
Preclinical
Authors
Loading...
Remains preclinical; extends biophysical models of HV1 gating but leaves open human translation.
Trp207 is crucial for the unique biophysical properties of the human voltage-gated proton channel, including slow opening, proton selectivity, and pH-dependent gating.
Cherny et al. (2015) studied this question. Mutation of Trp207 (to Ala, Ser, or Phe) vs. Wild-type (WT) hHV1 channels was evaluated on Channel gating kinetics and activation energy. Replacing Trp207 in human HV1 with Ala, Ser, or Phe accelerated channel opening by 100-fold and decreased activation energy from 30-38 kcal/mol to 22 kcal/mol, indicating Trp207 favors a closed state.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: