Two-pore domain potassium channels (K2P) control excitability, stabilize the resting
membrane potential below firing threshold, and accelerate repolarisation in different cells. Until
now, fifteen different genes for the six K2P channel subfamily were cloned. The pore-forming
part is translated from two genes and they are built up from a dimer of two two-unit transmembrane
domains functioning with a wide spectrum of physiological profiles. K2P ion channels
were discovered in the last two decades and gave novel opportunity to recognize the complex
molecular mechanism of the potassium ion flux, and may lead to the design of individual drug
targeting in the future. In this review, we summarise the structure, function, channelopathies
and pharmacological silhouette of the two-pore potassium channels in the human tissues. In
addition, we present the computer model of the partially reconstructed wild type K2P1/TWIK1
lacking the intracellular C and N terminal loop