Kalium 3.0 is a comprehensive depository of natural, artificial, and labeled polypeptides acting on potassium channels

Abstract

Here, we introduce the third release of Kalium database (http://kaliumdb.org/), a manually curated comprehensive depository that accumulates data on polypeptide ligands of potassium channels. The major goal of this amplitudinous update is to summarize findings for natural polypeptide ligands of K+ channels, as well as data for the artificial derivatives of these substances obtained over the decades of exploration. We manually analyzed more than 700 original manuscripts and systematized the information on mutagenesis, production of radio‐ and fluorescently labeled derivatives, and the molecular pharmacology of K+ channel ligands. In result, data on more than 1200 substances were processed and added enriching the database content fivefold. We also included the electrophysiological data obtained on the understudied and neglected K+ channels including the heteromeric and concatenated channels. We associated target channels in Kalium with corresponding entries in the official database of the International Union of Basic and Clinical Pharmacology (IUPHAR). Kalium was supplemented with an adaptive Statistics page, where users are able to obtain actual data output. Several other improvements were introduced, such as a color code to distinguish the range of ligand activity concentrations and advanced tools for filtration and sorting. Kalium is a fully open‐access database, crosslinked to other databases of interest. It can be utilized as a convenient resource containing ample up‐to‐date information about polypeptide ligands of K+ channels.This article is protected by copyright. All rights reserved.

The scorpion toxin BeKm‐1 blocks hERG cardiac potassium channels using an indispensable arginine residue

“…There is a great diversity of K + -channel isoforms, and scorpion peptide toxins blocking K + -channels (KTx) are seen as convenient tools to study this diversity. Despite a conserved CSa/b fold with three or four disulfide bridges, KTx are capable of distinguishing various K + -channel families, including K v , K Ca , and K ir [2,3]. For instance, there are peptides specific to either Shaker (K v 1) or human Ether-a-go-go-Related Gene (hERG or K v 11) channels, which belong to a-KTx and c-KTx toxin families, respectively.…”