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Curr Opin Struct Biol. 2015 Aug;33:68-75. doi: 10.1016/j.sbi.2015.07.012. Epub 2015 Aug 15.

A structural biology perspective on NMDA receptor pharmacology and function.

Author information

1
Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States.
2
Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States; Watson School of Biological Sciences, United States.
3
Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory, United States; Watson School of Biological Sciences, United States. Electronic address: furukawa@cshl.edu.

Abstract

N-methyld-aspartate receptors (NMDARs) belong to the large family of ionotropic glutamate receptors (iGluRs), which are critically involved in basic brain functions as well as multiple neurological diseases and disorders. The NMDARs are large heterotetrameric membrane protein complexes. The extensive extracellular domains recognize neurotransmitter ligands and allosteric compounds and translate the binding information to regulate activity of the transmembrane ion channel. Here, we review recent advances in the structural biology of NMDARs with a focus on pharmacology and function. Structural analysis of the isolated extracellular domains in combination with the intact heterotetrameric NMDAR structure provides important insights into how this sophisticated ligand-gated ion channel may function.

PMID:
26282925
PMCID:
PMC4641752
DOI:
10.1016/j.sbi.2015.07.012
[Indexed for MEDLINE]
Free PMC Article

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