Article
A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability.
Nature communications - 14 Sept 2018
Amin Johansen B, Leng Xiaoling, Gochman Aaron, Zhou Huan-Xiang, Wollmuth Lonnie P
Abstract excerpt
A variety of de novo and inherited missense mutations associated with neurological disorders are found in the NMDA receptor M4 transmembrane helices, which are peripheral to the pore domain in eukaryotic ionotropic glutamate receptors. Subsets of these mutations affect receptor gating with dramatic effects, including in one instance halting it, occurring at a conserved glycine near the extracellular end of M4....
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