Ligand-induced conformational changes in a SMALP-encapsulated GPCR.

ABSTRACT: The adenosine 2A receptor (A_2AR), a G-protein-coupled receptor (GPCR), was solubilised and purified encapsulated in styrene maleic acid lipid particles (SMALPs). The purified A_2AR-SMALP was associated with phospholipids characteristic of the plasma membrane of Pichia pastoris, the host used for its expression, confirming that the A_2AR-SMALP encapsulated native lipids. The fluorescence spectrum of the A_2AR-SMALP showed a characteristic broad emission peak at 330 nm, produced by endogenous Trp residues. The inverse agonist ZM241385 caused 30% increase in fluorescence emission, unusually accompanied by a red-shift in the emission wavelength. The emission spectrum also showed sub-peaks at 321 nm, 335 nm and 350 nm, indicating that individual Trp inha

SUBMITTER: Routledge SJ 

PROVIDER: S-EPMC7156913 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature