The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes.

ABSTRACT: Dynamic structural transitions within the seven-transmembrane bundle represent the mechanism by which G-protein-coupled receptors convert an extracellular chemical signal into an intracellular biological function. Here, the conformational dynamics of the neuropeptide Y receptor type 2 (Y2R) during activation was investigated. The apo, full agonist-, and arrestin-bound states of Y2R were prepared by cell-free expression, functional refolding, and reconstitution into lipid membranes. To study conformational transitions between these states, all six tryptophans of Y2R were ¹³ C-labeled. NMR-signal assignment was achieved by dynamic-nuclear-polarization enhancement and the individual functional states of the receptor were characterized by monitoring ¹³ C NMR chemical shif

SUBMITTER: Krug U 

PROVIDER: S-EPMC7736470 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature