P2X receptors

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Overview

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P2X receptors (nomenclature as agreed by NC-IUPHAR Subcommittee on P2X Receptors, [3,18]) have a trimeric topology [14,17,27] with two putative TM domains, gating primarily Na+, K+ and Ca2+, exceptionally Cl-. The Nomenclature Subcommittee has recommended that for P2X receptors, structural criteria should be the initial criteria for nomenclature where possible. Functional P2X receptors exist as polymeric transmitter-gated channels; the native receptors may occur as either homopolymers (e.g. P2X1 in smooth muscle) or heteropolymers (e.g. P2X2:P2X3 in the nodose ganglion and P2X1:P2X5 in mouse cortical astrocytes, [22]). P2X2, P2X4 and P2X7 receptors have been shown to form functional homopolymers which, in turn, activate pores permeable to low molecular weight solutes [33]. The hemi-channel pannexin-1 has been implicated in the pore formation induced by P2X7 [29], but not P2X2 [2], receptor activation.

Subunits

P2X1 Show summary » More detailed page

P2X2 Show summary » More detailed page

P2X3 Show summary » More detailed page

P2X4 Show summary » More detailed page

P2X5 Show summary » More detailed page

P2X6 Show summary » More detailed page

P2X7 Show summary » More detailed page

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NC-IUPHAR subcommittee and family contributors

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How to cite this family page

Database page citation:

P2X receptors. Accessed on 23/08/2014. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=77.

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Spedding M, Peters JA and Harmar AJ, CGTP Collaborators. (2013) The Concise Guide to PHARMACOLOGY 2013/14: Ligand-Gated Ion Channels. Br J Pharmacol. 170: 1582–1606.