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Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor

By Gregory V. Nikiforovich and R. Marshall

Abstract

ABSTRACT: A novel approach that iteratively combined the results of energy calculations and experimental data was used to generate a three-dimensional (3D) model of the photoactivated state (R*) of bovine rhodopsin (Rh). The approach started with simplified energy calculations in an effort to find a set of sterically and energetically reasonable options for transmembrane (TM) helix arrangements with all-trans-retinal. Various 3D models of TM helix packing found by computations were then compared to limited site-directed spin-label experimental data regarding the transition of the TM helices of Rh in the inactive state (R) to those in the R * state to identify the most plausible model of the TM helical bundle. At the next step, all non-TM structural elements, such as the non-TM helix 8, the N- and C-terminal fragments, and the loops connecting TM helices, were reconstructed, and after the entire R * structure had been relaxed, all other currently available additional experimental data, both mutational and spectroscopic, on the structure of the meta-II state of rhodopsin were used to validate the resulting 3D model. Rhodopsin (Rh),1 the 348-residue seven-transmembrane R-helical photoreceptor of the visual system, is the prototype for a vast subclass of G-protein-coupled receptors (GPCRs). The chromophore for this receptor is retinal that is covalentl

Year: 2015
OAI identifier: oai:CiteSeerX.psu:10.1.1.657.8427
Provided by: CiteSeerX
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