Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP.

ABSTRACT: Voltage-sensor domains (VSDs) are specialized transmembrane segments that confer voltage sensitivity to many proteins such as ion channels and enzymes. The activities of these domains are highly dependent on both the chemical properties and the physical properties of the surrounding membrane environment. To learn about VSD-lipid interactions, we used nuclear magnetic resonance spectroscopy to determine the structure and phospholipid interface of the VSD from the voltage-dependent K(+) channel KvAP (prokaryotic Kv from Aeropyrum pernix). The solution structure of the KvAP VSD solubilized within phospholipid micelles is similar to a previously determined crystal structure solubilized by a nonionic detergent and complexed with an antibody fragment. The differences observed include a previousl

SUBMITTER: Butterwick JA 

PROVIDER: S-EPMC2971526 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature