title: Purification and Crystallization of a Thermostabilized Agonist-Bound Conformation of the Human Adenosine A(2A) Receptor.
abstract: Crystallization of G protein-coupled receptors (GPCRs) is successful due to the development of generic protein engineering strategies, which has resulted in the structure determination of more than 25 GPCRs, including representatives from class A, B, C, and F. Most of the X-ray structures available correspond to an inactive conformation of the receptor bound to an antagonist. Only a few high-resolution structures of agonist-bound conformations of GPCRs have been determined over the last 6 years. Here, we describe the purification and crystallization protocols of a thermostabilized agonist-bound conformation of the human adenosine A2A receptor.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK, cgt@mrc-lmb.cam.ac.uk.
authors.forename: Christopher G
authors.initials: CG
authors.lastname: Tate
authors.forename: Guillaume
authors.initials: G
authors.lastname: Lebon
mesh_terms: D058908:Adenosine A2 Receptor Agonists / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D005591:Chemical Fractionation / Q000379:methods*; D003460:Crystallization; D006801:Humans; D011487:Protein Conformation; D055550:Protein Stability; D043705:Receptor, Adenosine A2A / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature; D014835:Volatilization
chemical_list: D058908:Adenosine A2 Receptor Agonists; D043705:Receptor, Adenosine A2A