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Ligand‐activated ion channels may share common gating mechanisms with the Shaker potassium channel
Author(s) -
Lee Chyuan-Yih
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81372-s
Subject(s) - shaker , chemistry , gating , biophysics , ligand gated ion channel , potassium channel , ion channel , protein subunit , agonist , nmda receptor , nicotinic acetylcholine receptor , nicotinic agonist , biochemistry , receptor , biology , physics , quantum mechanics , gene , vibration
This paper proposes a detailed gating mechanism for the N ‐methyl‐ d ‐aspartate (NMDA) channel. In the NMDARI subunit, the signal of agonist binding may be carried from Y456 to W590 through an electron transport chain, including W480 which could be the glycine modulatory site. The channel's opening may arise from repulsion between negatively charged W590s, analogous to W435s or the Shaker K + channel. The cyclic nucleotide‐gated channels may be activated by a similar mechanism, but the opening of nicotinic acetylcholine receptor (nAChR) channels is likely to be initiated by the formation of tyrosine radicals. The role of disulfide‐bonded cysteines in the redox modulation can also be explained.