Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure.

ABSTRACT: Rhodopsin is the only member of the pharmacologically important superfamily of G-protein-coupled receptors with a known structure at atomic resolution. A molecular dynamics model of rhodopsin in a POPC phospholipid bilayer was simulated for 15 ns, revealing a conformation significantly different from the recent crystal structures. The structure of the bilayer compared with a protein-free POPC control indicated hydrophobic matching with the nonpolar interface of the receptor, in agreement with deuterium NMR experiments. A new generalized molecular surface method, based on a three-dimensional Voronoi cell construction for atoms with different radii, was developed to quantify cross-sectional area profiles for the protein, lipid acyl chains and headgroups, and water. Thus, it was possible to i

SUBMITTER: Huber T 

PROVIDER: S-EPMC1304060 | biostudies-literature | 2004 Apr

REPOSITORIES: biostudies-literature