Literature DB >> 15123543

Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure.

Nathan L Absalom1, Trevor M Lewis, Peter R Schofield.   

Abstract

The nicotinic-like ligand-gated ion channel superfamily consists of a group of structurally related receptors that activate an ion channel after the binding of extracellular ligand. The recent publications of the crystal structure of an acetylcholine binding protein and a refined electron micrograph structure of the membrane-bound segment of an acetylcholine receptor have led to insights into the molecular determinants of receptor function. Although the structures confirmed much biochemical and electrophysiological data obtained about the receptors, they also provide opportunities to study further the mechanisms that allow channel activation stimulated by ligand-binding. Here we review the mechanisms of channel gating that have been elucidated by information gained from the structures of the acetylcholine binding protein and membrane-bound segment of the acetylcholine receptor.

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Year:  2004        PMID: 15123543     DOI: 10.1113/expphysiol.2003.026815

Source DB:  PubMed          Journal:  Exp Physiol        ISSN: 0958-0670            Impact factor:   2.969


  19 in total

1.  Molecular requirements for ethanol differential allosteric modulation of glycine receptors based on selective Gbetagamma modulation.

Authors:  Gonzalo E Yevenes; Gustavo Moraga-Cid; Ariel Avila; Leonardo Guzmán; Maximiliano Figueroa; Robert W Peoples; Luis G Aguayo
Journal:  J Biol Chem       Date:  2010-07-20       Impact factor: 5.157

2.  A gating mechanism proposed from a simulation of a human alpha7 nicotinic acetylcholine receptor.

Authors:  Richard J Law; Richard H Henchman; J Andrew McCammon
Journal:  Proc Natl Acad Sci U S A       Date:  2005-04-27       Impact factor: 11.205

3.  Acetylcholine nicotinic receptors: finding the putative binding site of allosteric modulators using the "blind docking" approach.

Authors:  Bogdan Iorga; Denyse Herlem; Elvina Barré; Catherine Guillou
Journal:  J Mol Model       Date:  2005-12-22       Impact factor: 1.810

4.  Functional asymmetry of transmembrane segments in nicotinic acetylcholine receptors.

Authors:  Jörg Grandl; Christophe Danelon; Ruud Hovius; Horst Vogel
Journal:  Eur Biophys J       Date:  2006-07-13       Impact factor: 1.733

5.  Ligand-induced conformational change in the alpha7 nicotinic receptor ligand binding domain.

Authors:  Richard H Henchman; Hai-Long Wang; Steven M Sine; Palmer Taylor; J Andrew McCammon
Journal:  Biophys J       Date:  2005-01-21       Impact factor: 4.033

6.  An energy-efficient gating mechanism in the acetylcholine receptor channel suggested by molecular and Brownian dynamics.

Authors:  Ben Corry
Journal:  Biophys J       Date:  2005-11-11       Impact factor: 4.033

7.  The pre-M1 segment of the alpha1 subunit is a transduction element in the activation of the GABAA receptor.

Authors:  Angelo Keramidas; Thomas L Kash; Neil L Harrison
Journal:  J Physiol       Date:  2006-06-08       Impact factor: 5.182

8.  Photo-activated azi-etomidate, a general anesthetic photolabel, irreversibly enhances gating and desensitization of gamma-aminobutyric acid type A receptors.

Authors:  Huijun Zhong; Dirk Rüsch; Stuart A Forman
Journal:  Anesthesiology       Date:  2008-01       Impact factor: 7.892

9.  Trans-cis switching mechanisms in proline analogues and their relevance for the gating of the 5-HT3 receptor.

Authors:  Claudio Melis; Giovanni Bussi; Sarah C R Lummis; Carla Molteni
Journal:  J Phys Chem B       Date:  2009-09-03       Impact factor: 2.991

10.  Covalent trapping of methyllycaconitine at the α4-α4 interface of the α4β2 nicotinic acetylcholine receptor: antagonist binding site and mode of receptor inhibition revealed.

Authors:  Nathan L Absalom; Gracia Quek; Trevor M Lewis; Taima Qudah; Ida von Arenstorff; Joseph I Ambrus; Kasper Harpsøe; Nasiara Karim; Thomas Balle; Malcolm D McLeod; Mary Chebib
Journal:  J Biol Chem       Date:  2013-07-26       Impact factor: 5.157

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