scholarly journals Identification of a Tyrosine in the Agonist Binding Site of the Homomeric ρ1 γ-Aminobutyric Acid (GABA) Receptor That, When Mutated, Produces Spontaneous Opening

2002 ◽  
Vol 277 (46) ◽  
pp. 43741-43748 ◽  
Author(s):  
Viviana I. Torres ◽  
David S. Weiss
Keyword(s):  
Binding Site ◽  
Gaba Receptor ◽  
Aminobutyric Acid ◽  
Agonist Binding

Structural elements involved in activation of the γ-aminobutyric acid type A (GABAA) receptor

2004 ◽  
Vol 32 (3) ◽  
pp. 540-546 ◽  
Author(s):  
T.L. Kash ◽  
J.R. Trudell ◽  
N.L. Harrison
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
Binding Site ◽  
Type A ◽  
Aminobutyric Acid ◽  
Structural Elements ◽  
Agonist Binding ◽  
Acid Type ◽  
Gated Ion Channels ◽  
Ligand Gated Ion Channels

Ligand-gated ion channels function as rapid signal transducers, converting chemical signals (in the form of neurotransmitters) into electrical signals in the postsynaptic neuron. This is achieved by the recognition of neurotransmitter at its specific-binding sites, which then triggers the opening of an ion channel (‘gating’). For this to occur rapidly (<1 ms), there must be an efficient coupling between the agonist-binding site and the gate, located more than 30 Å (1 Å=0.1 nm) away. Whereas a great deal of progress has been made in elucidating the structure and function of both the agonist-binding site and the ion permeation pathway in ligand-gated ion channels, our knowledge of the coupling mechanism between these domains has been limited. In this review, we summarize recent studies of the agonist-binding site and the ion channel in the γ-aminobutyric acid type A receptor, and discuss those structural elements that may mediate coupling between them. We will also consider some possible molecular mechanisms of receptor activation.

Locating GABA in GABA receptor binding sites

2009 ◽  
Vol 37 (6) ◽  
pp. 1343-1346 ◽  
Author(s):  
Sarah C.R. Lummis
Keyword(s):  
Ion Channels ◽  
Ligand Binding ◽  
Binding Site ◽  
Receptor Binding ◽  
Functional Data ◽  
Binding Sites ◽  
Gaba Receptor ◽  
Aminobutyric Acid ◽  
Specific Interactions ◽  
Gabac Receptors

The Cys-loop family of ligand-gated ion channels contains both vertebrate and invertebrate members that are activated by GABA (γ-aminobutyric acid). Many of the residues that are critical for ligand binding have been identified in vertebrate GABAA and GABAC receptors, and specific interactions between GABA and some of these residues have been determined. In the present paper, I show how a cation–π interaction for one of the binding site residues has allowed the production of models of GABA docked into the binding site, and these orientations are supported by mutagenesis and functional data. Surprisingly, however, the residue that forms the cation–π interaction is not conserved, suggesting that GABA occupies subtly different locations even in such closely related receptors.

scholarly journals A molecular characterization of the agonist binding site of a nematode cys-loop GABA receptor

2015 ◽  
Vol 172 (15) ◽  
pp. 3737-3747 ◽  
Author(s):  
Mark D Kaji ◽  
Ariel Kwaka ◽  
Micah K Callanan ◽  
Humza Nusrat ◽  
Jean-Paul Desaulniers ◽  
...  
Keyword(s):  
Binding Site ◽  
Molecular Characterization ◽  
Gaba Receptor ◽  
Agonist Binding

m-Sulfonate Benzene Diazonium Chloride: A Powerful Affinity Label for the ?-Aminobutyric Acid Binding Site from Rat Brain

1992 ◽  
Vol 59 (4) ◽  
pp. 1405-1413 ◽  
Author(s):  
Marie-Jeanne Bouchet ◽  
Patrice Jacques ◽  
Brigitte Ilien ◽  
Maurice Goeldner ◽  
Christian Hirth
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Aminobutyric Acid ◽  
Affinity Label ◽  
Benzene Diazonium

Phenobarbitone modulation of postsynaptic GABA receptor function on cultured mammalian neurons

1979 ◽  
Vol 206 (1164) ◽  
pp. 319-327 ◽  
Keyword(s):  
Time Constant ◽  
Gaba Receptor ◽  
Aminobutyric Acid ◽  
Current Fluctuations ◽  
Receptor Function ◽  
Spinal Neurons ◽  
Synaptic Currents ◽  
Open Time ◽  
Postsynaptic Action ◽  
The Mean

The anticonvulsant barbiturate phenobarbitone increases membrane current and conductance responses to γ-aminobutyric acid (GABA) in cultured mouse spinal neurons. Analyses of GABA current fluctuations under control conditions and in the presence of phenobarbitone show that the principle action is to increase the average time during which GABA- activated channels remain open. The duration of miniature synaptic currents with a time constant of decay similar to the mean open-time of GABA-activated channels is prolonged by the drug. The results suggest that (1) the synaptic events are GABA-mediated and (2) the enhancement of these events by barbiturate is due to the postsynaptic action of the drug.

Homology modeling in tandem with 3D-QSAR analyses: A computational approach to depict the agonist binding site of the human CB2 receptor

2011 ◽  
Vol 46 (9) ◽  
pp. 4489-4505 ◽  
Author(s):  
Elena Cichero ◽  
Alessia Ligresti ◽  
Marco Allarà ◽  
Vincenzo di Marzo ◽  
Zelda Lazzati ◽  
...  
Keyword(s):  
Homology Modeling ◽  
Binding Site ◽  
3D Qsar ◽  
Computational Approach ◽  
Agonist Binding ◽  
Cb2 Receptor
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