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A Chimeric GPCR Model Mimicking the Ligand Binding Site of the Human Y1 Receptor Studied by NMR Spectroscopy
Author(s) -
Walser Reto,
Kleinschmidt Jörg H.,
Zerbe Oliver
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100244
Subject(s) - g protein coupled receptor , nuclear magnetic resonance spectroscopy , ligand (biochemistry) , computational biology , chemistry , scaffold , receptor , fusion protein , binding site , scaffold protein , cooperative binding , spectroscopy , combinatorial chemistry , biophysics , stereochemistry , computer science , biochemistry , recombinant dna , biology , physics , gene , signal transduction , database , quantum mechanics
Graft order: The putative binding epitopes of peptides of the NPY family at their cognate GPCR, the Y1 receptor, were grafted onto a stable β‐barrel scaffold. We demonstrate the synthetic feasibility of such an approach and discuss its potential benefits. The integrity of the scaffold as well as its interaction with NPY was studied by using solution NMR spectroscopy.