Structure of a glutamate-receptor ligand-binding core in complex with kainate

Neali Armstrong; Yu Sun; Guo-Qiang Chen; Eric Gouaux

doi:10.1038/27692

journal article Oct 01, 1998

Structure of a glutamate-receptor ligand-binding core in complex with kainate

Neali Armstrong Yu Sun

Guo-Qiang Chen Eric Gouaux

Nature Vol. 395 No. 6705 pp. 913-917 · Springer Science and Business Media LLC

View at Publisher Save 10.1038/27692

Topics

No keywords indexed for this article. Browse by subject →

References

29

[1]

Hollmann, M. & Heinemann, S. Cloned glutamate receptors. Annu. Rev. Neurosci. 17, 31–108 (1994). 10.1146/annurev.ne.17.030194.000335

[2]

Rogers, S. W. et al. Autoantibodies to glutamate receptor GluR3 in Rasmussen's encephalitis. Science 265, 648–651 (1994). 10.1126/science.8036512

[3]

Stern-Bach, Y. et al. Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13, 1345–1357 (1994). 10.1016/0896-6273(94)90420-0

[4]

Kuusinen, A., Arvola, M. & Keinänen, K. Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J. 14, 6327–6332 (1995). 10.1002/j.1460-2075.1995.tb00323.x

[5]

Paas, Y. The macro- and microarchitectures of the ligand-binding domain of glutamate receptors. Trends Neurosci. 21, 117–125 (1998). 10.1016/s0166-2236(97)01184-3

[6]

Chen, G.-Q., Sun, Y., Jin, R. & Gouaux, E. Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct. Protein Sci. (in the press). 10.1002/pro.5560071216

[7]

Sommer, B. et al. Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS. Science 249, 1580–1585 (1990). 10.1126/science.1699275

[8]

Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51–58 (1991). 10.1126/science.1925561

[9]

Nakanishi, N., Shneider, N. A. & Axel, R. Afamily of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Neuron 5, 569–581 (1990). 10.1016/0896-6273(90)90212-x

[10]

Sun, Y.-J., Rose, J., Wang, B.-C. & Hsiao, C.-D. The structure of glutamine-binding protein complexed with glutamine at 1.94 å resolution: comparisons with other amino acid binding proteins. J. Mol. Biol. 278, 219–229 (1998). 10.1006/jmbi.1998.1675

[11]

Keinänen, K., Arvola, M., Kuusinen, A. & Johnson, M. Ligand recognition in glutamate receptors: insights from mutagenesis of the soluble α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-binding domain of glutamate receptor type D (GluR-D). Biochem. Soc. Trans. 25, 835–838 (1997). 10.1042/bst0250835

[12]

Laube, B., Hirai, H., Sturgess, M., Betz, H. & Kuhse, J. Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit. Neuron 18, 493–503 (1997). 10.1016/s0896-6273(00)81249-0

[13]

Paas, Y., Eisenstein, M., Medevielle, F., Teichberg, V. I. & Devillers-Thiéry, A. Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor. Neuron 17, 979–990 (1996). 10.1016/s0896-6273(00)80228-7

[14]

Hirai, H., Kirsch, J., Laube, B., Betz, H. & Kuhse, J. The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Proc. Natl Acad. Sci. USA 93, 6031–6036 (1996). 10.1073/pnas.93.12.6031

[15]

Swanson, G. T., Gereau, R. W. IV, Green, T. & Heinemann, S. F. Identification of amino acid residues that control functional behavior in GluR5 and GluR6 kainate receptors. Neuron 19, 913–926 (1997). 10.1016/s0896-6273(00)80972-1

[16]

Jacobson, B. L., He, J. J., Lemon, D. D. & Quiocho, F. A. Interdomain salt bridges modulate ligand-induced domain motion of the sulfate receptor protein for active transport. J. Mol. Biol. 223, 27–30 (1992). 10.1016/0022-2836(92)90712-s

[17]

Li, F., Owens, N. & Verdoorn, T. A. Functional effects of mutations in the putative agonist binding region of recombinant α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. Mol. Pharmacol. 47, 148–154 (1995).

[18]

Aizenman, E., Lipton, S. A. & Loring, R. H. Selective modulation of NMDA responses by reduction and oxidation. Neuron 2, 1257–1263 (1989). 10.1016/0896-6273(89)90310-3

[19]

Sutcliffe, M. J., Wo, Z. G. & Oswald, R. E. Three-dimensional models of non-NMDA glutamate receptors. Biophys. J. 70, 1575–1589 (1996). 10.1016/s0006-3495(96)79724-2

[20]

Partin, K. M., Bowie, D. & Mayer, M. L. Structural determinants of allosteric regulation in alternatively spliced AMPA receptors. Neuron 14, 833–843 (1995). 10.1016/0896-6273(95)90227-9

[21]

Partin, K. M., Fleck, M. W. & Mayer, M. L. AMPA receptor flip/flop mutants affecting deactivation, desensitization, and modulation by cyclothiazide, aniracetam, and thiocyanate. J. Neurosci. 16, 6634–6647 (1996). 10.1523/jneurosci.16-21-06634.1996

[22]

[20] Processing of X-ray diffraction data collected in oscillation mode

Zbyszek Otwinowski, Wladek Minor

Methods in Enzymology 1997 10.1016/s0076-6879(97)76066-x

[23]

Cowtan, K. D. & Main, P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D 42, 43–48 (1996). 10.1107/s090744499500761x

[24]

Read, R. J. Model phases: probabilities and bias. Methods Enzymol. 277, 110–128 (1997). 10.1016/s0076-6879(97)77009-5

[25]

Jones, T. A. & Kjeldgaard, M. Electron-density map interpretation. Methods Enzymol. 277, 173–208 (1997). 10.1016/s0076-6879(97)77012-5

[26]

Brünger, A. T. X-PLOR. Version 3.1. A System for X-ray Crystallography and NMR 1–382 (Yale Univ. Press, New Haven, 1992).

[27]

The CCP4 suite: programs for protein crystallography

Collaborative Computational Project, Number 4

Acta Crystallographica Section D Biological Crysta... 10.1107/s0907444994003112

[28]

Hollmann, M., Maron, C. & Heinemann, S. N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13, 1331–1343 (1994). 10.1016/0896-6273(94)90419-7

[29]

Lomeli, H. et al. Control of kinetic properties of AMPA receptor channels by nuclear RNA editing. Science 266, 1709–1713 (1994). 10.1126/science.7992055

Cited By

555

Exploring the regulatory roles of AtGLR3.4 receptors in mitochondrial stress and ROS management in Arabidopsis

Azime Gokce, Askim Hediye Sekmen · 2025

Plant Cell Reports

Improved Parameterization of Amine–Carboxylate and Amine–Phosphate Interactions for Molecular Dynamics Simulations Using the CHARMM and AMBER Force Fields

Jejoong Yoo, Aleksei Aksimentiev · 2015

Journal of Chemical Theory and Comp...

X-ray structures of AMPA receptor–cone snail toxin complexes illuminate activation mechanism

Lei Chen, Katharina L. Dürr · 2014

Science

Defining the structural relationship between kainate-receptor deactivation and desensitization

G Brent Dawe, Maria Musgaard · 2013

Nature Structural & Molecular B...

Biostructural and Pharmacological Studies of Bicyclic Analogues of the 3-Isoxazolol Glutamate Receptor Agonist Ibotenic Acid

Karla Frydenvang, Darryl S. Pickering · 2010

Journal of Medicinal Chemistry

Glutamate Receptor Ion Channels: Structure, Regulation, and Function

Stephen F. Traynelis, Lonnie P. Wollmuth · 2010

Pharmacological Reviews

Ancient Protostome Origin of Chemosensory Ionotropic Glutamate Receptors and the Evolution of Insect Taste and Olfaction

Vincent Croset, Raphael Rytz · 2010

PLOS Genetics

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

Alexander I. Sobolevsky, Michael P. Rosconi · 2009

Nature

The sequence of events that underlie quantal transmission at central glutamatergic synapses

John E. Lisman, Sridhar Raghavachari · 2007

Nature Reviews Neuroscience

Ionotropic and metabotropic glutamate receptor structure and pharmacology

James N. C. Kew, John A. Kemp · 2005

Psychopharmacology

Mass Spectrometry as a Tool for Protein Crystallography

Steven L. Cohen, Brian T. Chait · 2001

Annual Review of Biophysics and Bio...

Conversion of a maltose receptor into a zinc biosensor by computational design

Jonathan S. Marvin, Homme W. Hellinga · 2001

Proceedings of the National Academy...

Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled Receptors

Ulrik Gether · 2000

Endocrine Reviews

Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

Naoki Kunishima, Yoshimi Shimada · 2000

Nature

Four Residues of the Extracellular N-Terminal Domain of the NR2A Subunit Control High-Affinity Zn2+ Binding to NMDA Receptors

Amir Fayyazuddin, Alvaro Villarroel · 2000

Neuron

The Glutamate Receptor Ion Channels

Raymond Dingledine, Karin Borges · 1999

Pharmacological Reviews

Functional characterization of a potassium-selective prokaryotic glutamate receptor

Guo-Qiang Chen, Changhai Cui · 1999

Nature

The venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors

Christian B. Felder, Richard C. Graul · 1999

AAPS PharmSci

Metrics

555

Citations

29

References

Details

Published: Oct 01, 1998
Vol/Issue: 395(6705)
Pages: 913-917
License: View

Authors

Zhejiang University

Howard Hughes Medical Institute

Cite This Article

Neali Armstrong, Yu Sun, Guo-Qiang Chen, et al. (1998). Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature, 395(6705), 913-917. https://doi.org/10.1038/27692

Structure of a glutamate-receptor ligand-binding core in complex with kainate

You May Also Like