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PROSITE documentation PDOC00932

ATP P2X receptors signature





Description

P2X purinoreceptors [1,2] are cation-selective ion channels that open on binding to extracellular ATP; they play a role in fast synaptic transmission between neurones, and from autonomic nerves to smooth muscles. When ATP is released as a neurotransmitter from central and peripheral nerves it acts at P2X receptors to produce postsynaptic depolarization and excitation.

P2X receptors are from 397 to 595 amino acids long. They consist of a short intracellular N-terminus region followed by a transmembrane domain, a large extracellular loop that contains 10 conserved cysteines, a second transmembrane segment and a C-terminal intracellular tail.

Currently, seven forms (P2X1 to P2X7) of P2X receptors are known.

As a signature pattern, we selected a conserved region located in the central part of the extracellular domain and which contains two of the conserved cysteines.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

November 1997 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

P2X_RECEPTOR, PS01212; ATP P2X receptors signature  (PATTERN)


References

1AuthorsSurprenant A. Buell G.N. North R.A.
TitleP2X receptors bring new structure to ligand-gated ion channels.
SourceTrends Neurosci. 18:224-229(1995).
PubMed ID7541920

2AuthorsKennedy C. Leff P.
TitleHow should P2X purinoceptors be classified pharmacologically?
SourceTrends Pharmacol. Sci. 16:168-174(1995).
PubMed ID7624972



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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