PROSITE documentation PDOC00932 [for PROSITE entry PS01212]ATP P2X receptors signature
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.
Last update:November 1997 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Surprenant A. Buell G.N. North R.A. |
| Title | P2X receptors bring new structure to ligand-gated ion channels. | |
| Source | Trends Neurosci. 18:224-229(1995). | |
| PubMed ID | 7541920 |
| 2 | Authors | Kennedy C. Leff P. |
| Title | How should P2X purinoceptors be classified pharmacologically? | |
| Source | Trends Pharmacol. Sci. 16:168-174(1995). | |
| PubMed ID | 7624972 |
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