Simulations of a G protein-coupled receptor homology model predict dynamic features and a ligand binding site
| Autor: | Marcus Böckmann, Klaus Gerwert, Udo Höweler, Steffen Wolf, Jürgen Schlitter |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Rhodopsin Epinephrine Biophysics Sequence alignment Crystallography X-Ray Ligands Biochemistry Homology (biology) Molecular dynamics GPCR Structural Biology Computational chemistry Molecular dynamics simulation Genetics Point Mutation Computer Simulation Amino Acid Sequence Homology modeling Molecular Biology Ligand binding G protein-coupled receptor Homology model Binding Sites biology Chemistry Beta(2) adrenoreceptor Cell Biology Structural Homology Protein biology.protein Receptors Adrenergic beta-2 Biological system |
| Zdroj: | FEBS Letters. 582:3335-3342 |
| ISSN: | 0014-5793 |
| Popis: | A computational approach to predict structures of rhodopsin-like G protein-coupled receptors (GPCRs) is presented and evaluated by comparison to the X-ray structural models. By combining sequence alignment, the rhodopsin crystal structure, and point mutation data on the β2 adrenoreceptor (b2ar), we predict a (−)-epinephrine-bound computational model of the β2 adrenoreceptor. The model is evaluated by molecular dynamics simulations and by comparison with the recent X-ray structures of b2ar. The overall correspondence between the predicted and the X-ray structural model is high. Especially the prediction of the ligand binding site is accurate. This shows that the proposed dynamic homology modelling approach can be used to create reasonable models for the understanding of structure and dynamics of other rhodopsin-like GPCRs. |
| Databáze: | OpenAIRE |
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