Regulation of AMPA Receptor Gating by Ligand Binding Core Dimers

Neuron

Volumn 41, Issue 3, 2004, Pages 379-388

  Horning, Michelle S ^a,b   Mayer, Mark L ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; DIMER; GLUTAMATE RECEPTOR;

ACCELERATION; ARTICLE; CHANNEL GATING; CLUSTER ANALYSIS; CRYSTAL STRUCTURE; DESENSITIZATION; HUMAN; HYDROGEN BOND; MUTAGENESIS; MUTANT; NONHUMAN; PATCH CLAMP; PRIORITY JOURNAL; PROTEIN BINDING; RECORDING; REGULATORY MECHANISM; ULTRACENTRIFUGATION;

EID: 1242293631     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(04)00018-2     Document Type: Article

References (24)

1. Abele R., Keinanen K., Madden D.R. Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis. J. Biol. Chem. 275:2000;21355-21363.
2. Armstrong N., Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor. Crystal structures of the GluR2 ligand binding core Neuron. 28:2000;165-181.
3. Armstrong N., Sun Y., Chen G.Q., Gouaux E. Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature. 395:1998;913-917.
4. Armstrong N., Mayer M., Gouaux E. Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes. Proc. Natl. Acad. Sci. USA. 100:2003;5736-5741.
5. Brejc K., van Dijk W.J., Klaassen R.V., Schuurmans M., van der Oost J., Smit A.B., Sixma T.K. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature. 411:2001;269-276.
6. Chen C., Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:1987;2745-2752.
7. Chen G.Q., Cui C., Mayer M.L., Gouaux E. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature. 402:1999;817-821.
8. Dingledine R., Borges K., Bowie D., Traynelis S.F. The glutamate receptor ion channels. Pharmacol. Rev. 51:1999;7-45.
9. Fleck M.W., Cornell E., Mah S.J. Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization. J. Neurosci. 23:2003;1219-1227.
10. Furukawa H., Gouaux E. Mechanisms of activation, inhibition and specificity. Crystal structures of NR1 ligand-binding core EMBO J. 22:2003;1-13.
11. Hogner A., Greenwood J.R., Liljefors T., Lunn M.L., Egebjerg J., Larsen I.K., Gouaux E., Kastrup J.S. Competitive antagonism of AMPA receptors by ligands of different classes. crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX J. Med. Chem. 46:2003;214-221.
12. Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;515-522.
13. Jin R., Gouaux E. Probing the function, conformational plasticity, and dimer-dimer contacts of the GluR2 ligand-binding core. Studies of 5-substituted willardiines and GluR2 S1S2 in the crystal Biochemistry. 42:2002;5201-5213.
14. Jin R., Horning M., Mayer M.L., Gouaux E. Mechanism of activation and selectivity in a ligand-gated ion channel. structural and functional studies of GluR2 and quisqualate Biochemistry. 41:2002;15635-15643.
15. Jin R., Banke T.G., Mayer M.L., Traynelis S.F., Gouaux E. Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6:2003;803-810.
16. Kraulis P.J. Molscript. A program to produce both detailed and schematic plots of protein structures J. App. Crystal. 24:1991;946-950.
17. Kuusinen A., Abele R., Madden D.R., Keinanen K. Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5- methyl-4-isoxazole propionic acid receptor subunit GluRD. J. Biol. Chem. 274:1999;28937-28943.
18. Mayer M.L., Olson R., Gouaux E. Mechanisms for ligand binding to GluR0 ion channels. Crystal structures of the glutamate and serine complexes and a closed apo state J. Mol. Biol. 311:2001;815-836.
19. Merritt E.A., Bacon D.J. Raster3D. Photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
20. Miyazawa A., Fujiyoshi Y., Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 424:2003;949-955.
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. 16:1996;6634-6647.
22. Stern-Bach Y., Bettler B., Hartley M., Sheppard P.O., O'Hara P.J., Heinemann S.F. Agonist-selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid binding proteins. Neuron. 13:1994;1345-1357.
23. Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E. Mechanism of glutamate receptor desensitization. Nature. 417:2002;245-253.
24. Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R., Gouaux E. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature. 425:2003;200-205.