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TitleStructural Mechanism of Functional Modulation by Gene Splicing in NMDA Receptors.
Journal, issue, pagesNeuron, Vol. 98, Issue 3, Page 521-529.e3, Year 2018
Publish dateMay 2, 2018
AuthorsMichael C Regan / Timothy Grant / Miranda J McDaniel / Erkan Karakas / Jing Zhang / Stephen F Traynelis / Nikolaus Grigorieff / Hiro Furukawa /
PubMed AbstractAlternative gene splicing gives rise to N-methyl-D-aspartate (NMDA) receptor ion channels with defined functional properties and unique contributions to calcium signaling in a given chemical ...Alternative gene splicing gives rise to N-methyl-D-aspartate (NMDA) receptor ion channels with defined functional properties and unique contributions to calcium signaling in a given chemical environment in the mammalian brain. Splice variants possessing the exon-5-encoded motif at the amino-terminal domain (ATD) of the GluN1 subunit are known to display robustly altered deactivation rates and pH sensitivity, but the underlying mechanism for this functional modification is largely unknown. Here, we show through cryoelectron microscopy (cryo-EM) that the presence of the exon 5 motif in GluN1 alters the local architecture of heterotetrameric GluN1-GluN2 NMDA receptors and creates contacts with the ligand-binding domains (LBDs) of the GluN1 and GluN2 subunits, which are absent in NMDA receptors lacking the exon 5 motif. The unique interactions established by the exon 5 motif are essential to the stability of the ATD/LBD and LBD/LBD interfaces that are critically involved in controlling proton sensitivity and deactivation.
External linksNeuron / PubMed:29656875 / PubMed Central
MethodsEM (single particle)
Resolution4.6 Å
Structure data

7529

6cna

EMDB-7529, PDB-6cna:
GluN1-GluN2B NMDA receptors with exon 5
Method: EM (single particle) / Resolution: 4.6 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / Splicing variant

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