Inward-rectifier potassium channel
| Inward rectifier potassium channel | |||||||
|---|---|---|---|---|---|---|---|
crystal structure of an inward rectifier potassium channel | |||||||
| Identifiers | |||||||
| Symbol | IRK | ||||||
| Pfam | PF01007 | ||||||
| Pfam clan | CL0030 | ||||||
| InterPro | IPR013521 | ||||||
| SCOP2 | 1n9p / SCOPe / SUPFAM | ||||||
| TCDB | 1.A.2 | ||||||
| OPM superfamily | 8 | ||||||
| OPM protein | 3SPG | ||||||
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Inward-rectifier potassium channels (Kir, IRK) are a specific lipid-gated subset of potassium channels. To date, seven subfamilies have been identified in various mammalian cell types, plants, and bacteria. They are activated by phosphatidylinositol 4,5-bisphosphate (PIP2). The malfunction of the channels has been implicated in several diseases. IRK channels possess a pore domain, homologous to that of voltage-gated ion channels, and flanking transmembrane segments (TMSs). They may exist in the membrane as homo- or heterooligomers and each monomer possesses between 2 and 4 TMSs. In terms of function, these proteins transport potassium (K+), with a greater tendency for K+ uptake than K+ export. The process of inward-rectification was discovered by Bernard Katz in skeletal muscle cells in 1949, and Denis Noble in cardiac muscle cells in 1960s.