Arginine 199 and leucine 208 have key roles in the control of adenosine A2A receptor signalling function.

ABSTRACT: One successful approach to obtaining high-resolution crystal structures of G-protein coupled receptors is the introduction of thermostabilising mutations within the receptor. This technique allows the generation of receptor constructs stabilised into different conformations suitable for structural studies. Previously, we functionally characterised a number of mutants of the adenosine A2A receptor, thermostabilised either in an agonist or antagonist conformation, using a yeast cell growth assay and demonstrated that there is a correlation between thermostability and loss of constitutive activity. Here we report the functional characterisation of 30 mutants intermediate between the Rag23 (agonist conformation mutant) and the wild-type receptor using the same yeast signalling assay with the a

SUBMITTER: Bertheleme N 

PROVIDER: S-EPMC3940607 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature