Open AccessTwo P domain potassium channels in GtoPdb v.2021.2
Author(s) -
Austin M. Baggetta,
Douglas A. Bayliss,
Gábor Czirják,
Péter Enyedi,
Steve A.N. Goldstein,
Florian Lesage,
Daniel L. Minor,
Leigh D. Plant,
Francisco V. Sepúlveda,
Brenda T. Winn
Publication year - 2021
Publication title -
iuphar/bps guide to pharmacology cite
Language(s) - English
Resource type - Journals
ISSN - 2633-1020
DOI - 10.2218/gtopdb/f79/2021.2
Subject(s) - potassium channel , protein subunit , ion channel , nomenclature , biophysics , potassium , chemistry , biology , biochemistry , receptor , taxonomy (biology) , zoology , gene , organic chemistry
The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two P domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below.