Mechanisms of sodium/calcium selectivity in sodium channels probed by cysteine mutagenesis and sulfhydryl modification.

@article{PrezGarca1997MechanismsOS,
  title={Mechanisms of sodium/calcium selectivity in sodium channels probed by cysteine mutagenesis and sulfhydryl modification.},
  author={M Teresa P{\'e}rez-Garc{\'i}a and Nipavan Chiamvimonvat and Ravi Ranjan and Jeffrey R. Balser and Gordon F. Tomaselli and Eduardo Marb{\'a}n},
  journal={Biophysical journal},
  year={1997},
  volume={72 3},
  pages={989-96}
}
A conserved lysine residue in the "P loop" of domain III renders sodium channels highly selective. Conversion of this residue to glutamate, to mimic the homologous position in calcium channels, enables Ca2+ to permeate sodium channels. Because the lysine-to-glutamate mutation converts a positively charged side chain to a negative one, it has been proposed that a positive charge at this position suffices for Na+ selectivity. We tested this idea by converting the critical lysine to cysteine… CONTINUE READING

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