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

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

Biophysical journal - 21 May 2013

Dai Jian, Zhou Huan-Xiang

Abstract excerpt

N-methyl-D-aspartate (NMDA) receptors are obligate heterotetrameric ligand-gated ion channels that play critical roles in learning and memory. Here, using targeted molecular dynamics simulations, we developed an atomistic model for the gating of the GluN1/GluN2A NMDA receptor. Upon agonist binding, lobe closure of the ligand-binding domain produced outward pulling of the M3-D2 linkers, leading to outward...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Calcium
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mice, Neurologic Mutants

Share to Molecular Dynamics Simulation

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Receptors, N-Methyl-D-Aspartate

Source

Open in PubMed Open full text

Identifiers

PMID: 23708357
DOI: 10.1016/j.bpj.2013.04.013
PMCID: PMC3660646

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.PMID 23708357Read ↗

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain.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 ↗

Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.Semantic proximity Read ↗

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

Arrangement of subunits in functional NMDA receptors.Semantic proximity Read ↗

Cross-subunit Interactions that Stabilize Open States Mediate Gating in NMDA ReceptorsSemantic proximity Read ↗

Complex functional phenotypes of NMDA receptor disease variantsSemantic proximity Read ↗

Probing the Structural Dynamics of the NMDA Receptor Activation by Coarse-Grained Modeling.Semantic proximity Read ↗

Complex functional phenotypes of NMDA receptor disease variantsSemantic proximity Read ↗

Recovery from desensitization in GluA2 AMPA receptors is affected by a single mutation in the N-terminal domain interface.Semantic proximity Read ↗

The GluN2B-Glu413Gly NMDA receptor variant arising from a de novo GRIN2B mutation promotes ligand-unbinding and domain opening.Semantic proximity Read ↗

Computationally Discovered Potentiating Role of Glycans on NMDA Receptors.Semantic proximity Read ↗

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