Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain.

Structure (London, England : 1993) - 1 Oct 2007

Lau Albert Y, Roux Benoît

Abstract excerpt

Ionotropic glutamate receptors are ligand-gated transmembrane ion channels activated by the binding of glutamate. The free energy landscapes governing the opening/closing of the GluR2 S1S2 ligand-binding domain in the apo, DNQX-, and glutamate-bound forms are computed by using all-atom molecular dynamics simulations with explicit solvent, in conjunction with an umbrella sampling strategy. The apo S1S2 easily...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apoproteins
Share to Glutamic Acid
Share to Ligands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Quinoxalines

Share to Receptors, AMPA

Share to Scattering, Small Angle

Share to Thermodynamics

Share to X-Ray Diffraction

Source

Open in PubMed Open full text

Identifiers

PMID: 17937910
DOI: 10.1016/j.str.2007.07.015
PMCID: PMC2288668

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain.PMID 17937910Read ↗

D-Serine Potently Drives Ligand-Binding Domain Closure in the Ionotropic Glutamate Receptor GluD2.Semantic proximity Read ↗

An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Semantic proximity Read ↗

Configurational Preference of the Glutamate Receptor Ligand Binding Domain Dimers.Semantic proximity Read ↗

The Free Energy Landscape of GABA Binding to a Pentameric Ligand-Gated Ion Channel and Its Disruption by Mutations.Semantic proximity Read ↗

Steered Molecular Dynamics Simulations Predict Conformational Stability of Glutamate Receptors.Semantic proximity Read ↗

Binding and Dynamics Demonstrate the Destabilization of Ligand Binding for the S688Y Mutation in the NMDA Receptor GluN1 Subunit.Semantic proximity Read ↗

Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct.Semantic proximity Read ↗

The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.Semantic proximity Read ↗

Computational design of constitutively active mutants of Dopamine D2 receptor inspired by ligand-independent activation mechanisms.Semantic proximity Read ↗

Effects of Familial Alzheimer's Disease Mutations on the Folding Free Energy and Dipole-Dipole Interactions of the Amyloid β-Peptide.Semantic proximity Read ↗

Disruption of interdomain interactions in the glutamate binding pocket affects differentially agonist affinity and efficacy of N-methyl-D-aspartate receptor activation.Semantic proximity Read ↗

Molecular dynamics simulation of the truncated NMDA receptor in the open stateSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.