(Q27654089)

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Mechanisms of Antagonism of the GluR2 AMPA Receptor: Structure and Dynamics of the Complex of Two Willardiine Antagonists with the Glutamate Binding Domain

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scholarly article

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Mechanisms of Antagonism of the GluR2 AMPA Receptor: Structure and Dynamics of the Complex of Two Willardiine Antagonists with the Glutamate Binding Domain (English)

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Holger Sondermann

7

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author name string

Ahmed H Ahmed

1

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Melissa D Thompson

2

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Michael K Fenwick

3

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Bethsabe Romero

4

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Adrienne P Loh

5

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David E Jane

6

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Robert E Oswald

8

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language of work or name

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publication date

12 May 2009

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48

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18

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3894-903

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Structure of the S1S2 glutamate binding domain of GLuR3

1 reference

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20 March 2017

TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists

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20 March 2017

Structural basis for partial agonist action at ionotropic glutamate receptors

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20 March 2017

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

1 reference

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20 March 2017

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes

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20 March 2017

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

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20 March 2017

Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate

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20 March 2017

Mechanism of glutamate receptor desensitization

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20 March 2017

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

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20 March 2017

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

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20 March 2017

Version 1.2 of the Crystallography and NMR system

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PHENIX: building new software for automated crystallographic structure determination

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20 March 2017

The glutamate receptor ion channels

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20 March 2017

Ionotropic glutamate receptors. Their possible role in the expression of hippocampal synaptic plasticity

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20 March 2017

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7 April 2017

Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists

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20 March 2017

Cloned glutamate receptors

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7 April 2017

Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2693247

29 September 2017

NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists

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29 September 2017

The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain

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29 September 2017

Allosteric mechanism in AMPA receptors: a FRET-based investigation of conformational changes

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29 September 2017

Glutamate receptors at atomic resolution

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29 September 2017

Synthesis and pharmacology of willardiine derivatives acting as antagonists of kainate receptors.

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29 September 2017

Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen

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29 September 2017

Synthesis of willardiine and 6-azawillardiine analogs: pharmacological characterization on cloned homomeric human AMPA and kainate receptor subtypes

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29 September 2017

Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain

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2 June 2018

Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct

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2 June 2018

The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209.

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Microsecond-to-millisecond conformational dynamics demarcate the GluR2 glutamate receptor bound to agonists glutamate, quisqualate, and AMPA.

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/19284741

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1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1021/BI900107M

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