Ontology highlight
ABSTRACT:
SUBMITTER: Streit AK
PROVIDER: S-EPMC3077598 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Streit Anne K AK Netter Michael F MF Kempf Franca F Walecki Magdalena M Rinné Susanne S Bollepalli Murali K MK Preisig-Müller Regina R Renigunta Vijay V Daut Jürgen J Baukrowitz Thomas T Sansom Mark S P MS Stansfeld Phillip J PJ Decher Niels N
The Journal of biological chemistry 20110301 16
Two-pore domain potassium (K(2P)) channels play a key role in setting the membrane potential of excitable cells. Despite their role as putative targets for drugs and general anesthetics, little is known about the structure and the drug binding site of K(2P) channels. We describe A1899 as a potent and highly selective blocker of the K(2P) channel TASK-1. As A1899 acts as an open-channel blocker and binds to residues forming the wall of the central cavity, the drug was used to further our understa ...[more]