A single aspartate residue is involved in both intrinsic gating and blockage by Mg2+ of the inward rectifier, IRK1.

@article{Stanfield1994ASA,
  title={A single aspartate residue is involved in both intrinsic gating and blockage by Mg2+ of the inward rectifier, IRK1.},
  author={Peter R. Stanfield and Noel W Davies and Pauline Shelton and Michael J. Sutcliffe and Ikhlas A Khan and W. J. Brammar and Edward C. Conley},
  journal={The Journal of physiology},
  year={1994},
  volume={478 ( Pt 1)},
  pages={
          1-6
        }
}
1. We describe the effects on channel function of changing an aspartate residue (Asp172) in a membrane-spanning alpha-helix of the murine inward rectifier, IRK1, by site-directed mutagenesis. 2. Alteration of Asp172 to Glu (charged) or to Gln or Asn (polar but uncharged) produced functional channels showing inward rectification, though rectification was weaker with Gln and Asn. 3. Intrinsic gating around the potassium equilibrium potential, EK, was conserved only if the charge on residue 172… CONTINUE READING
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