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

Agonist trapped in ATP-binding sites of the P2X2 receptor.

Proceedings of the National Academy of Sciences of the United States of America - 31 May 2011

Jiang Ruotian, Lemoine Damien, Martz Adeline, Taly Antoine, Gonin Sophie, Prado de Carvalho Lia, Specht Alexandre, Grutter Thomas

Abstract excerpt

ATP-gated P2X receptors are trimeric ion channels, as recently confirmed by X-ray crystallography. However, the structure was solved without ATP and even though extracellular intersubunit cavities surrounded by conserved amino acid residues previously shown to be important for ATP function were p...

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 Biophysics
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to DNA, Complementary

Share to Ligands

Share to Patch-Clamp Techniques

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 21576497
DOI: 10.1073/pnas.1102170108
PMCID: PMC3107266

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21576497-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Agonist trapped in ATP-binding sites of the P2X2 receptor.PMID 21576497Read ↗

Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor.Semantic proximity Read ↗

Conformational flexibility of the agonist binding jaw of the human P2X3 receptor is a prerequisite for channel opening.Semantic proximity Read ↗

Activation of trimeric P2X2 receptors by fewer than three ATP molecules.Semantic proximity Read ↗

Molecular dissection of purinergic P2X receptor channels.Semantic proximity Read ↗

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

Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors.Semantic proximity Read ↗

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

Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Semantic proximity Read ↗

Molecular Structure and Regulation of P2X Receptors With a Special Emphasis on the Role of P2X2 in the Auditory System.Semantic proximity Read ↗

Salt bridge switching from Arg290/Glu167 to Arg290/ATP promotes the closed-to-open transition of the P2X2 receptor.Semantic proximity Read ↗

Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domain.Semantic 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 ↗

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