Mechanism of NMDA receptor channel block by MK-801 and memantine

Song, Xianqiang; Jensen, Morten Ø.; Jogini, Vishwanath; Stein, Richard A.; Lee, Chia-Hsueh; Mchaourab, Hassane S.; Shaw, David E.; Gouaux, Eric

doi:10.1038/s41586-018-0039-9

Title: Mechanism of NMDA receptor channel block by MK-801 and memantine

Journal Article · Wed Apr 18 00:00:00 EDT 2018 · Nature (London)

DOI:https://doi.org/10.1038/s41586-018-0039-9· OSTI ID:1435812

Song, Xianqiang ^[1]; Jensen, Morten Ø. ^[2]; Jogini, Vishwanath ^[2]; Stein, Richard A. ^[3]; Lee, Chia-Hsueh ^[1]; Mchaourab, Hassane S. ^[3]; Shaw, David E. ^[4]; Gouaux, Eric ^[1]

Oregon Health & Science Univ., Portland, OR (United States)
D. E. Shaw Research, New York, NY (United States)
Vanderbilt Univ., Nashville, TN (United States)
Columbia Univ., New York, NY (United States)

The NMDA (N-methyl-d-aspartate) receptor transduces the binding of glutamate and glycine, coupling it to the opening of a calcium-permeable ion channel. Owing to the lack of high-resolution structural studies of the NMDA receptor, the mechanism by which ion-channel blockers occlude ion permeation is not well understood. Here we show that removal of the amino-terminal domains from the GluN1–GluN2B NMDA receptor yields a functional receptor and crystals with good diffraction properties, allowing us to map the binding site of the NMDA receptor blocker, MK-801. Here, this crystal structure, together with long-timescale molecular dynamics simulations, shows how MK-801 and memantine (a drug approved for the treatment of Alzheimer’s disease) bind within the vestibule of the ion channel, promote closure of the ion channel gate and lodge between the M3-helix-bundle crossing and the M2-pore loops, physically blocking ion permeation.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Inst. of Health

Grant/Contract Number:: R01 NS038631

OSTI ID:: 1435812

Journal Information:: Nature (London), Vol. 556, Issue 7702; ISSN 0028-0836

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 122 works

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