A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability.
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ABSTRACT:
SUBMITTER: Amin JB
PROVIDER: S-EPMC6138751 | biostudies-literature | 2018 Sep
REPOSITORIES: biostudies-literature
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A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca<sup>2+</sup> permeability.
Amin Johansen B JB Leng Xiaoling X Gochman Aaron A Zhou Huan-Xiang HX Wollmuth Lonnie P LP
Nature communications 20180914 1
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. Functional experiments and molecular dynamic simulations of constructs with and withou ...[more]
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