Defining the interface between the C-terminal fragment of alpha-transducin and photoactivated rhodopsin.

ABSTRACT: A novel combination of experimental data and extensive computational modeling was used to explore probable protein-protein interactions between photoactivated rhodopsin (R*) and experimentally determined R*-bound structures of the C-terminal fragment of alpha-transducin (Gt(alpha)(340-350)) and its analogs. Rather than using one set of loop structures derived from the dark-adapted rhodopsin state, R* was modeled in this study using various energetically feasible sets of intracellular loop (IC loop) conformations proposed previously in another study. The R*-bound conformation of Gt(alpha)(340-350) and several analogs were modeled using experimental transferred nuclear Overhauser effect data derived upon binding R*. Gt(alpha)(340-350) and its analogs were docked to various conformations of t

SUBMITTER: Taylor CM 

PROVIDER: S-EPMC1877773 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature