Thermodynamic Characterization of New Positive Allosteric Modulators Binding to the Glutamate Receptor A2 Ligand-Binding Domain: Combining Experimental and Computational Methods Unravels Differences in Driving Forces

2014 ◽  
Vol 54 (12) ◽  
pp. 3404-3416 ◽  
Author(s):  
Ann-Beth Nørholm ◽  
Pierre Francotte ◽  
Eric Goffin ◽  
Iuliana Botez ◽  
Laurence Danober ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Glutamate Receptor ◽  
Computational Methods ◽  
Driving Forces ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Allosteric Modulators ◽  
Thermodynamic Characterization ◽  
Positive Allosteric Modulators

scholarly journals Crystal Structures of Potent Dimeric Positive Allosteric Modulators at the Ligand-Binding Domain of the GluA2 Receptor

2018 ◽  
Vol 10 (3) ◽  
pp. 243-247
Author(s):  
Saara Laulumaa ◽  
Kathrine Voigt Hansen ◽  
Magdalena Masternak ◽  
Thomas Drapier ◽  
Pierre Francotte ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Crystal Structures ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Allosteric Modulators ◽  
Positive Allosteric Modulators

scholarly journals Exploring the Role of Positive Allosteric Modulators in Stabilizing the GluR2 Ligand-Binding Domain Dimer

2010 ◽  
Vol 98 (3) ◽  
pp. 609a
Author(s):  
Christopher P. Ptak ◽  
Ahmed H. Ahmed ◽  
Michael K. Fenwick ◽  
Alexander S. Maltsev ◽  
Robert E. Oswald
Keyword(s):  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Allosteric Modulators ◽  
Positive Allosteric Modulators

scholarly journals Zinc Potentiates GluK3 Glutamate Receptor Function by Stabilizing the Ligand Binding Domain Dimer Interface

Neuron ◽  
2012 ◽  
Vol 76 (3) ◽  
pp. 565-578 ◽  
Author(s):  
Julien Veran ◽  
Janesh Kumar ◽  
Paulo S. Pinheiro ◽  
Axel Athané ◽  
Mark L. Mayer ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Glutamate Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Receptor Function ◽  
Dimer Interface

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

2000 ◽  
Vol 267 (13) ◽  
pp. 4281-4289 ◽  
Author(s):  
Dean R. Madden ◽  
Rupert Abele ◽  
Arnold Andersson ◽  
Kari Keinänen
Keyword(s):  
Glutamate Receptor ◽  
Receptor Agonist ◽  
Large Scale ◽  
Binding Domain ◽  
Agonist Binding ◽  
Thermodynamic Characterization ◽  
Glutamate Receptor Agonist

scholarly journals Systematic and functional characterization of novel androgen receptor variants arising from alternative splicing in the ligand-binding domain

Oncogene ◽  
2016 ◽  
Vol 36 (10) ◽  
pp. 1440-1450 ◽  
Author(s):  
T Uo ◽  
H Dvinge ◽  
C C Sprenger ◽  
R K Bradley ◽  
P S Nelson ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Alternative Splicing ◽  
Ligand Binding ◽  
Functional Characterization ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Androgen Receptor Variants

scholarly journals Structural Mechanisms Underlying Activity Changes in an AMPA-type Glutamate Receptor Induced by Substitutions in Its Ligand-Binding Domain

Structure ◽  
2019 ◽  
Vol 27 (11) ◽  
pp. 1698-1709.e5
Author(s):  
Masayoshi Sakakura ◽  
Yumi Ohkubo ◽  
Hiraku Oshima ◽  
Suyong Re ◽  
Masahiro Ito ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Glutamate Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Structural Mechanisms

scholarly journals Characterization of the Nurr1 ligand-binding domain co-activator interaction surface

2006 ◽  
Vol 37 (2) ◽  
pp. 317-326 ◽  
Author(s):  
Nikolaos Volakakis ◽  
Michal Malewicz ◽  
Banafsheh Kadkhodai ◽  
Thomas Perlmann ◽  
Gerard Benoit
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Close Association ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Site Directed Mutagenesis ◽  
Orphan Nuclear Receptor ◽  
Hydrophobic Region ◽  
Binding Surface

The recently solved crystal structure of the orphan nuclear receptor (NR) Nurr1 ligand-binding domain (LBD) showed that Nurr1 lacks a cavity for ligand binding and a canonical NR co-activator-binding site. Computer modeling of the Nurr1 LBD structure identified a hydrophobic region on the surface of the Nurr1 LBD that was positioned on the opposite side from the classical co-activator-binding site. Site-directed mutagenesis demonstrated that this region is critical for the activity of the Nurr1 LBD. Most mutations introduced in this region reduced or abolished transcriptional activity of the Nurr1 LBD, but mutation at lysine (K577) resulted in a drastically increased activity. Moreover, the activity of the Nurr1 LBD was shown to correlate with a propensity for proteasome-dependent degradation revealing a close association between activity and Nurr1 protein turnover. These data provide novel insights into the mechanisms of transcription via the Nurr1 LBD and identify an alternative co-activator-binding surface that is unique to the NR4A family of NRs.

Characterization of the Ligand-Binding Domain of the Ecdysteroid Receptor from Drosophila Melanogaster

2003 ◽  
Vol 384 (1) ◽  
Author(s):  
M. Grebe ◽  
S. Przibilla ◽  
V.C. Henrich ◽  
M. Spindler-Barth
Keyword(s):  
Drosophila Melanogaster ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Ecdysteroid Receptor
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