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

AI Article Synopsis

  • G-protein-coupled receptors, like the neuropeptide Y receptor type 2 (Y2R), change their structure to convert external chemical signals into actions inside the cell.
  • Researchers examined Y2R's structure in three states (inactive, fully activated, and arrestin-bound) using advanced techniques to understand how it switches between these states.
  • Key findings included the identification of crucial "toggle switches" in the receptor's structure, especially two tryptophan residues, which help facilitate its activation process.

Article 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 C-labeled. NMR-signal assignment was achieved by dynamic-nuclear-polarization enhancement and the individual functional states of the receptor were characterized by monitoring C NMR chemical shifts. Activation of Y2R is mediated by molecular switches involving the toggle switch residue Trp281 of the highly conserved SWLP motif and Trp327 adjacent to the NPxxY motif. Furthermore, a conformationally preserved "cysteine lock"-Trp116 was identified.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7736470PMC
http://dx.doi.org/10.1002/anie.202006075DOI Listing

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