The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Mechanism of NMDA receptor channel block by MK-801 and memantine
Open accessAbstract
The NMDA (N-methyl-d-aspartate) receptor transduces the binding of glutamate and glycine, coupling it to the opening of a calcium-permeable ion channel1. 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. 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. A high-resolution X-ray structure and molecular dynamics simulations of the N-methyl-d-aspartate receptor in complexes with channel-blocking ligands reveals the molecular basis of the ligand binding and channel block.
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Cited by
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686
Structure, function, and allosteric modulation of NMDA receptors
Hansen, K. B., Yi, F., Perszyk, R. E., Furukawa, H., Wollmuth, L. P., Gibb, A. J., & Traynelis, S. F. (2018) · Journal of General Physiology · doi:10.1085/jgp.201812032 · Cited by 573
The Role of NMDA Receptors in Alzheimer’s Disease
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Structural basis of ketamine action on human NMDA receptors
Zhang, Y., Ye, F., Zhang, T., Lv, S., Zhou, L., Du, D., Lin, H., Guo, F., Luo, C., & Zhu, S. (2021) · Nature · doi:10.1038/s41586-021-03769-9 · Cited by 218
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150
Metadata
- Authors
- Song, X., Jensen, M. Ø., Jogini, V., Stein, R. A., Lee, C.-H., Mchaourab, H. S., Shaw, D. E., & Gouaux, E.
- Venue
- Nature
- Published
- 2018-04
- Volume
- 556
- Issue
- 7702
- Pages
- 515-519
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2797071919
- Cited by
- 264
- References
- 55
- FWCI
- 11.49
- Type
- journal article
- Language
- en
- Open access
- green
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