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

Mechanism of the Association between Na+ Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium Symporters.

The Journal of biological chemistry - 29 May 2015

Stolzenberg Sebastian, Quick Matthias, Zhao Chunfeng, Gotfryd Kamil, Khelashvili George, Gether Ulrik, Loland Claus J, Javitch Jonathan A, Noskov Sergei, Weinstein Harel, Shi Lei

Abstract excerpt

Neurotransmitter:sodium symporters (NSSs) terminate neurotransmission by Na(+)-dependent reuptake of released neurotransmitters. Previous studies suggested that Na(+)-binding reconfigures dynamically coupled structural elements in an allosteric interaction network (AIN) responsible for function-related conformational changes, but the intramolecular pathway of this mechanism has remained uncharted. We describe a...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Dopamine Plasma Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lithium

Share to Metals

Share to Molecular Dynamics Simulation

Share to Neurotransmitter Agents

Share to Sodium

Source

Open in PubMed Open full text

Identifiers

PMID: 25869126
DOI: 10.1074/jbc.M114.625343
PMCID: PMC4447972

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism of the Association between Na+ Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium Symporters.PMID 25869126Read ↗

Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue.Semantic proximity Read ↗

Spontaneous Inward Opening of the Dopamine Transporter Is Triggered by PIP2-Regulated Dynamics of the N-TerminusSemantic proximity Read ↗

Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog.Semantic proximity Read ↗

Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuT.Semantic proximity Read ↗

Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.Semantic proximity Read ↗

Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site.Semantic proximity Read ↗

Interaction of GAT1 with sodium ions: from efficient recruitment to stabilisation of substrate and conformationSemantic proximity Read ↗

Atomic-level characterization of conformational transition and substrate binding of xCT transporterSemantic proximity Read ↗

Allosteric effects of the coupling cation in melibiose transporter MelBSemantic proximity Read ↗

Evolutionary analysis reveals the origin of sodium coupling in glutamate transportersSemantic proximity Read ↗

Unbiased simulations reveal the inward-facing conformation of the human serotonin transporter and Na(+) ion release.Semantic proximity Read ↗

Molecular mechanism of substrate specificity in the bacterial neutral amino acid transporter LeuT.Semantic proximity Read ↗

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