Atomistic Study of Intramolecular Interactions in the Closed-State Channelrhodopsin Chimera, C1C2.

ABSTRACT: Channelrhodopsins (ChR1 and ChR2) are light-activated ion channels that enable photomobility of microalgae from the genus Chlamydomonas. Despite common use of ChR2 in optogenetics for selective control and monitoring of individual neurons in living tissue, the protein structures remain unresolved. Instead, a crystal structure of the ChR chimera (C1C2), an engineered combination of helices I-V from ChR1, without its C-terminus, and helices VI-VII from ChR2, is used as a template for ChR2 structure prediction. Surprisingly few studies have focused in detail on the chimera. Here, we present atomistic molecular dynamics studies of the closed-state, non-conducting C1C2 structure and protonation states. A new and comprehensive characterization of interactions in the vicinity of the gating region

SUBMITTER: VanGordon MR 

PROVIDER: S-EPMC5355493 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature