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

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 D-Serine Potently Drives Ligand-Binding Domain Closure in the Ionotropic Glutamate Receptor GluD2

Structure ◽  
2020 ◽  
Vol 28 (10) ◽  
pp. 1168-1178.e2
Author(s):  
Alfred C. Chin ◽  
Remy A. Yovanno ◽  
Tyler J. Wied ◽  
Ariel Gershman ◽  
Albert Y. Lau
Keyword(s):  
Ligand Binding ◽  
Glutamate Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Ionotropic Glutamate Receptor

scholarly journals The GluK3 Ligand Binding Domain has a Zinc Binding Site at the Dimer Interface

2013 ◽  
Vol 104 (2) ◽  
pp. 272a
Author(s):  
Janesh Kumar ◽  
Julien Veran ◽  
Paulo S. Pinheiro ◽  
Axel Athane ◽  
David Perrais ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Zinc Binding ◽  
Dimer Interface ◽  
Zinc Binding Site

scholarly journals Agonist-induced Isomerization in a Glutamate Receptor Ligand-binding Domain

2000 ◽  
Vol 275 (28) ◽  
pp. 21355-21363 ◽  
Author(s):  
Rupert Abele ◽  
Kari Keinänen ◽  
Dean R. Madden
Keyword(s):  
Ligand Binding ◽  
Glutamate Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Receptor Ligand

scholarly journals Correlating efficacy and desensitization with GluK2 ligand-binding domain movements

Open Biology ◽  
2013 ◽  
Vol 3 (5) ◽  
pp. 130051 ◽  
Author(s):  
Naushaba Nayeem ◽  
Olga Mayans ◽  
Tim Green
Keyword(s):  
Ligand Binding ◽  
Conformational Changes ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Anion Binding ◽  
Charge Balance ◽  
Dimer Interface ◽  
Ligand Affinity ◽  
Cleft Closure ◽  
Binding Cleft

Gating of AMPA- and kainate-selective ionotropic glutamate receptors can be defined in terms of ligand affinity, efficacy and the rate and extent of desensitization. Crucial insights into all three elements have come from structural studies of the ligand-binding domain (LBD). In particular, binding-cleft closure is associated with efficacy, whereas dissociation of the dimer formed by neighbouring LBDs is linked with desensitization. We have explored these relationships in the kainate-selective subunit GluK2 by studying the effects of mutating two residues (K531 and R775) that form key contacts within the LBD dimer interface, but whose truncation unexpectedly attenuates desensitization. One mutation (K531A) also switches the relative efficacies of glutamate and kainate. LBD crystal structures incorporating these mutations revealed several conformational changes that together explain their phenotypes. K531 truncation results in new dimer contacts, consistent with slower desensitization and sideways movement in the ligand-binding cleft correlating with efficacy. The tested mutants also disrupted anion binding; no chloride was detected in the dimer-interface site, including in R775A where absence of chloride was the only structural change evident. From this, we propose that the charge balance in the GluK2 LBD dimer interface maintains a degree of instability, necessary for rapid and complete desensitization.

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