Structural and energetic effects of A2A adenosine receptor mutations on agonist and antagonist binding.

ABSTRACT: To predict structural and energetic effects of point mutations on ligand binding is of considerable interest in biochemistry and pharmacology. This is not only useful in connection with site-directed mutagenesis experiments, but could also allow interpretation and prediction of individual responses to drug treatment. For G-protein coupled receptors systematic mutagenesis has provided the major part of functional data as structural information until recently has been very limited. For the pharmacologically important A(2A) adenosine receptor, extensive site-directed mutagenesis data on agonist and antagonist binding is available and crystal structures of both types of complexes have been determined. Here, we employ a computational strategy, based on molecular dynamics free energy simulations

SUBMITTER: Keranen H 

PROVIDER: S-EPMC4186821 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature