Towards Probing Conformational States of Y2 Receptor Using Hyperpolarized ¹²⁹Xe NMR.

ABSTRACT: G protein-coupled receptors can adopt many different conformational states, each of them exhibiting different restraints towards downstream signaling pathways. One promising strategy to identify and quantify this conformational landscape is to introduce a cysteine at a receptor site sensitive to different states and label this cysteine with a probe for detection. Here, the application of NMR of hyperpolarized ¹²⁹Xe for the detection of the conformational states of human neuropeptide Y2 receptor is introduced. The xenon trapping cage molecule cryptophane-A attached to a cysteine in extracellular loop 2 of the receptor facilitates chemical exchange saturation transfer experiments without and in the presence of native ligand neuropeptide Y. High-quality spectra indicative of struct

SUBMITTER: Schmidt P 

PROVIDER: S-EPMC9919357 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature