Characterization of ligands for the human T1R2 sweet taste receptor (obtention "Manfred Rothe Poster Award")

2016

poster ayant obtenu le prix "Manfred Rothe Poster Award"; The human sweet-taste receptor is a heterodimer composed of two class C G-protein coupled receptors (GPCR), T1R2 and T1R3. Both subunits possess a large N-terminal domain (NTD) linked to a heptahelical transmembrane domain (TM) by a cysteine rich domain (CRD) [1]. Cellular assays, molecular docking and mutagenesis studies have revealed that small sweet ligands interact primarily with the NTD of T1R2 (T1R2-NTD) [2, 3]. To further elucidate the contribution of T1R2-NTD to small sweet ligand binding, we overexpressed T1R2-NTD in Escherichia coli as inclusion bodies [4, 5]. Human T1R2-NTD was refolded and the correct formation of seconda…