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Literature DB >> 22106178

Structure and function of glutamate receptor amino terminal domains.

Abstract

The amino terminal domain (ATD) of ionotropic glutamate receptor (iGluR) subunits resides at the extracellular region distal to the membrane. The ATD is structurally and functionally the most divergent region of the iGluR subunits. Structural studies on full-length GluA2 and the ATDs from three iGluR subfamilies have shed light on how the ATD facilitates subunit assembly, accommodates allosteric modulator compounds, and controls gating properties. Here recent developments in structural and functional studies on iGluR ATDs are reviewed.

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Year: 2011 PMID： 22106178 PMCID： PMC3300046 DOI： 10.1113/jphysiol.2011.213850

Source DB: PubMed Journal: J Physiol ISSN： 0022-3751 Impact factor: 5.182

52 in total

Review 1. Novel N-methyl-D-aspartate receptor antagonists: a review of compounds patented since 2006.

Authors: Manuel Koller; Stephan Urwyler
Journal: Expert Opin Ther Pat Date: 2010-11-08 Impact factor: 6.674

2. Subunit arrangement and function in NMDA receptors.

Authors: Hiroyasu Furukawa; Satinder K Singh; Romina Mancusso; Eric Gouaux
Journal: Nature Date: 2005-11-10 Impact factor: 49.962

3. Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.

Authors: Neali Armstrong; Jaysankar Jasti; Mads Beich-Frandsen; Eric Gouaux
Journal: Cell Date: 2006-10-06 Impact factor: 41.582

4. Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.

Authors: Marc Gielen; Anne Le Goff; David Stroebel; Jon W Johnson; Jacques Neyton; Pierre Paoletti
Journal: Neuron Date: 2008-01-10 Impact factor: 17.173

5. Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors.

Authors: Yongneng Yao; Chris B Harrison; Peter L Freddolino; Klaus Schulten; Mark L Mayer
Journal: EMBO J Date: 2008-07-17 Impact factor: 11.598

6. Mechanism of partial agonist action at the NR1 subunit of NMDA receptors.

Authors: Atsushi Inanobe; Hiroyasu Furukawa; Eric Gouaux
Journal: Neuron Date: 2005-07-07 Impact factor: 17.173

7. Mechanism of positive allosteric modulators acting on AMPA receptors.

Authors: Rongsheng Jin; Suzanne Clark; Autumn M Weeks; Joshua T Dudman; Eric Gouaux; Kathryn M Partin
Journal: J Neurosci Date: 2005-09-28 Impact factor: 6.167

8. Structure and different conformational states of native AMPA receptor complexes.

Authors: Terunaga Nakagawa; Yifan Cheng; Elizabeth Ramm; Morgan Sheng; Thomas Walz
Journal: Nature Date: 2005-02-03 Impact factor: 49.962

9. N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor.

Authors: Palmi T Atlason; Molly L Garside; Elisabeth Meddows; Paul Whiting; R A Jeffrey McIlhinney
Journal: J Biol Chem Date: 2007-07-02 Impact factor: 5.157

10. Extracellular interactions between GluR2 and N-cadherin in spine regulation.

Authors: Laura Saglietti; Caroline Dequidt; Kinga Kamieniarz; Marie-Claude Rousset; Pamela Valnegri; Olivier Thoumine; Francesca Beretta; Laurent Fagni; Daniel Choquet; Carlo Sala; Morgan Sheng; Maria Passafaro
Journal: Neuron Date: 2007-05-03 Impact factor: 17.173

20 in total

1. Ligand-gated ion channels: from genes to behaviour.

Authors: Derek Bowie
Journal: J Physiol Date: 2012-01-01 Impact factor: 5.182

2. Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.

Authors: Rita E Sirrieh; David M MacLean; Vasanthi Jayaraman
Journal: J Biol Chem Date: 2013-06-21 Impact factor: 5.157

3. Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.

Authors: Amy J Gleichman; Lynn A Spruce; Josep Dalmau; Steven H Seeholzer; David R Lynch
Journal: J Neurosci Date: 2012-08-08 Impact factor: 6.167

Structure and function of glutamate receptor amino terminal domains.

Review 1. Novel N-methyl-D-aspartate receptor antagonists: a review of compounds patented since 2006.

2. Subunit arrangement and function in NMDA receptors.

3. Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.

4. Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.

5. Molecular mechanism of ligand recognition by NR3 subtype glutamate receptors.

6. Mechanism of partial agonist action at the NR1 subunit of NMDA receptors.

7. Mechanism of positive allosteric modulators acting on AMPA receptors.

8. Structure and different conformational states of native AMPA receptor complexes.

9. N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor.

10. Extracellular interactions between GluR2 and N-cadherin in spine regulation.

1. Ligand-gated ion channels: from genes to behaviour.

2. Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.

3. Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.

Review 4. Structure and gating of tetrameric glutamate receptors.

Review 5. The multifaceted subunit interfaces of ionotropic glutamate receptors.

6. Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.

Review 7. Glutamatergic autoencephalitides: an emerging field.

Review 8. Emerging structural insights into the function of ionotropic glutamate receptors.

Review 9. Functional insights from glutamate receptor ion channel structures.

Review 10. A structural biology perspective on NMDA receptor pharmacology and function.