Coupled motions between pore and voltage-sensor domains: a model for Shaker B, a voltage-gated potassium channel.

ABSTRACT: A high-resolution crystal structure of KvAP, an archeabacterial voltage-gated potassium (Kv) channel, complexed with a monoclonal Fab fragment has been recently determined. Based on this structure, a mechanism for the activation (opening) of Kv channels has been put forward. This mechanism has since been criticized, suggesting that the resolved structure is not representative of the family of voltage-gated potassium channels. Here, we propose a model of the transmembrane domain of Shaker B, a well-characterized Kv channel, built by homology modeling and docking calculations. In this model, the positively charged S4 helices are oriented perpendicular to the membrane and localized in the groove between segments S5 and S6 of adjacent subunits. The structure and the dynamics of the full atomis

SUBMITTER: Treptow W 

PROVIDER: S-EPMC1304659 | biostudies-literature | 2004 Oct

REPOSITORIES: biostudies-literature