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

Unique residues in the ATP gated human P2X7 receptor define a novel allosteric binding pocket for the selective antagonist AZ10606120.

Scientific reports - 7 Apr 2017

Allsopp Rebecca C, Dayl Sudad, Schmid Ralf, Evans Richard J

Abstract excerpt

The P2X7 receptor (P2X7R) for ATP is a therapeutic target for pathophysiological states including inflammation, pain management and epilepsy. This is facilitated by the predicted low side effect profile as the high concentrations of ATP required to activate the receptor are usually only found following cell damage/disease and so P2X7Rs respond to a "danger" signal and are not normally active. AZ10606120 is a...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Allosteric Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Allosteric Site

Share to Aminoquinolines

Share to Ion Channel Gating

Share to Molecular Conformation

Share to Protein Interaction Domains and Motifs

Share to Receptors, Purinergic P2X7

Source

Open in PubMed Open full text

Identifiers

PMID: 28389651
DOI: 10.1038/s41598-017-00732-5
PMCID: PMC5429621

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

Unique residues in the ATP gated human P2X7 receptor define a novel allosteric binding pocket for the selective antagonist AZ10606120.PMID 28389651Read ↗

Mapping the binding site of P2X7 receptor antagonistsSemantic proximity Read ↗

Tyrosine 288 in the extracellular domain of the human P2X7 receptor is critical for receptor function revealed by structural modeling and site-directed mutagenesis.Semantic proximity Read ↗

Allosteric modulation of ATP-gated P2X receptor channels.Semantic proximity Read ↗

Structural insights into the allosteric inhibition of P2X4 receptorsSemantic proximity Read ↗

P2X7 Variants in PathophysiologySemantic proximity Read ↗

Contribution of Val/Ile87 residue in the extracellular domain in agonist-induced current responses of the human and rat P2X7 receptors.Semantic proximity Read ↗

Identification and characterization of splice variants of the human P2X7 ATP channel.Semantic proximity Read ↗

Cryo-EM reveals the structural basis of subtype-specific, noncompetitive inhibition of the human P2X3 receptorSemantic proximity Read ↗

P2X7 Receptor in Hematological MalignanciesSemantic proximity Read ↗

Scanning mutagenesis in a yeast system delineates the role of the NPxxY(x)(5,6)F motif and helix 8 of the adenosine A(2B) receptor in G protein coupling.Semantic proximity Read ↗

P2X2 receptor subunit interfaces are missense variant hotspots where mutations tend to increase apparent ATP affinitySemantic proximity Read ↗

Structural insights into the human P2X1 receptor and ligand interactionsSemantic proximity Read ↗

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