Molecular modeling of a tandem two pore domain potassium channel reveals a putative binding site for general anesthetics.

ABSTRACT: Anesthetics are thought to mediate a portion of their activity via binding to and modulation of potassium channels. In particular, tandem pore potassium channels (K2P) are transmembrane ion channels whose current is modulated by the presence of general anesthetics and whose genetic absence has been shown to confer a level of anesthetic resistance. While the exact molecular structure of all K2P forms remains unknown, significant progress has been made toward understanding their structure and interactions with anesthetics via the methods of molecular modeling, coupled with the recently released higher resolution structures of homologous potassium channels to act as templates. Such models reveal the convergence of amino acid regions that are known to modulate anesthetic activity onto a common

SUBMITTER: Bertaccini EJ 

PROVIDER: S-EPMC4306477 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature