Matches in SemOpenAlex for { <https://semopenalex.org/work/W4360610005> ?p ?o ?g. }
- W4360610005 abstract "Kinetics of NMDA receptor (NMDAR) ion channel opening and closing contribute to their unique role in synaptic signaling. Agonist binding generates free energy to open a canonical gate at the M3 helix bundle crossing. Single channel activity is characterized by clusters, or periods of rapid opening and closing, that are separated by long silent periods. A conserved glycine in the outer most transmembrane helices, the M4 helices, regulates NMDAR function. Here we find that the GluN1 glycine mainly regulates single channel events within a cluster, whereas the GluN2 glycine mainly regulates entry and exit from clusters. Molecular dynamics simulations suggest that, whereas the GluN2 M4 (along with GluN2 pre-M1) regulates the gate at the M3 helix bundle crossing, the GluN1 glycine regulates a 'gate' at the M2 loop. Subsequent functional experiments support this interpretation. Thus, the distinct kinetics of NMDARs are mediated by two gates that are under subunit-specific regulation." @default.
- W4360610005 created "2023-03-24" @default.
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- W4360610005 date "2023-03-23" @default.
- W4360610005 modified "2023-09-26" @default.
- W4360610005 title "Two gates mediate NMDA receptor activity and are under subunit-specific regulation" @default.
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- W4360610005 doi "https://doi.org/10.1038/s41467-023-37260-y" @default.
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