Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain

Ji Young Lee; James Krieger; Beatriz Herguedas; Javier García-Nafría; Anindita Dutta; Saher A. Shaikh; Ingo H. Greger; Ivet Bahar

doi:10.1016/j.str.2018.10.017

Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain

Ji Young Lee
, James Krieger
, Beatriz Herguedas
, Javier García-Nafría
, Anindita Dutta
, Saher A. Shaikh
, Ingo H. Greger
, Ivet Bahar

Laufer Center for Physical and Quantitative Biology

University of Pittsburgh
Medical Research Council

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Lee et al. assess the druggability of the ionotropic glutamate receptor subfamilies, using molecular dynamics simulations in the presence of drug-like molecules and X-ray crystallography. The study presents a ligand-binding site in the GluA3 N-terminal domain and supports the role of conformational plasticity in modulating ligand binding.

Original language	English
Pages (from-to)	241-252.e3
Journal	Structure
Volume	27
Issue number	2
DOIs	https://doi.org/10.1016/j.str.2018.10.017
State	Published - Feb 5 2019

Keywords

allosteric interactions
AMPA
druggability simulations
GluA3 N-terminal domain
ionotropic glutamate receptors
kainate receptors
ligand binding
molecular dynamics
NMDA
protein-protein interface

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10.1016/j.str.2018.10.017

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title = "Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain",

abstract = "Lee et al. assess the druggability of the ionotropic glutamate receptor subfamilies, using molecular dynamics simulations in the presence of drug-like molecules and X-ray crystallography. The study presents a ligand-binding site in the GluA3 N-terminal domain and supports the role of conformational plasticity in modulating ligand binding.",

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doi = "10.1016/j.str.2018.10.017",

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AU - Lee, Ji Young

AU - Krieger, James

AU - Herguedas, Beatriz

AU - García-Nafría, Javier

AU - Dutta, Anindita

AU - Shaikh, Saher A.

AU - Greger, Ingo H.

AU - Bahar, Ivet

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AB - Lee et al. assess the druggability of the ionotropic glutamate receptor subfamilies, using molecular dynamics simulations in the presence of drug-like molecules and X-ray crystallography. The study presents a ligand-binding site in the GluA3 N-terminal domain and supports the role of conformational plasticity in modulating ligand binding.

KW - allosteric interactions

KW - AMPA

KW - druggability simulations

KW - GluA3 N-terminal domain

KW - ionotropic glutamate receptors

KW - kainate receptors

KW - ligand binding

KW - molecular dynamics

KW - NMDA

KW - protein-protein interface

UR - https://www.scopus.com/pages/publications/85060732447

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JO - Structure

JF - Structure

IS - 2

ER -

Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain

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Keywords

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