The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins
Abstract
Receptors for the major excitatory neurotransmitter glutamate include metabotropic (G protein-coupled) and ionotropic (glutamate-gated ion channel) types. These receptors have large, presumably extracellular, amino-terminal domains. Sensitive sequence analysis techniques indicate that the metabotropic receptor extracellular domain is similar to bacterial periplasmic amino acid binding proteins. A structural model built using the observed similarity predicts a ligand-binding site, and mutants with conservative amino acid substitutions at this site are shown to have reduced ligand affinity. The metabotropic receptor extracellular domain is a member of a family of structural domains linked to a variety of receptor types, including ionotropic glutamate receptors.
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Cites
Improved tools for biological sequence comparison.
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Molecular cloning and characterization of the rat NMDA receptor
Moriyoshi, K., Masu, M., Ishii, T., Shigemoto, R., Mizuno, N., & Nakanishi, S. (1991) · Nature · doi:10.1038/354031a0 · Cited by 1,771
A Family of AMPA-Selective Glutamate Receptors
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A family of metabotropic glutamate receptors
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Cited by
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R. (2010) · Pharmacological Reviews · doi:10.1124/pr.109.002451 · Cited by 3,568
Glutamate receptors in the mammalian central nervous system
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A Multigene Family Encoding a Diverse Array of Putative Pheromone Receptors in Mammals
Matsunami, H., & Buck, L. B. (1997) · Cell · doi:10.1016/s0092-8674(00)80537-1 · Cited by 706
Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
Pin, J.-P., Galvez, T., & Prézeau, L. (2003) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(03)00038-x · Cited by 662
Aiba, A. (1994) · Cell · doi:10.1016/0092-8674(94)90204-6 · Cited by 614
Metadata
- Authors
- O'Hara, P. J., Sheppard, P. O., Thógersen, H., Venezia, D., Haldeman, B. A., McGrane, V., Houamed, K. M., Thomsen, C., Gilbert, T. L., & Mulvihill, E. R.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1993-07
- Volume
- 11
- Issue
- 1
- Pages
- 41-52
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2005913521
- Cited by
- 709
- References
- 5
- FWCI
- 11.47
- Type
- journal article
- Language
- en
- Open access
- closed
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- O'Hara, P. J., Sheppard, P. O., Thógersen, H., Venezia, D., Haldeman, B. A., McGrane, V., Houamed, K. M., Thomsen, C., Gilbert, T. L., & Mulvihill, E. R. (1993). The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins. Neuron. https://doi.org/10.1016/0896-6273(93)90269-w
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
