0000000000636621
AUTHOR
Fabrice Neiers
Ligand binding properties of OBP28a, a recombinant odorant binding protein from Drosophila melanogaster
National audience; Odorant binding proteins (OBPs) are small (around 14 kDa) soluble proteins isolated from the sensory organs of a wide range of insect species. OBP reversely bind odorants with dissociation constants in the micromolar range and are good candidate for transporting hydrophobic odorant molecules to olfactory receptors, through the aqueous sensillar lymph. In the genome of Drosophila melanogaster, 52 OBPs with high sequence divergence have been identified. Amongst them, OBP28a is one of the most abundant odorant binding proteins suggesting an important physiological role. A recent study proposed a novel role for this OBP in buffering changes in the odor environment (Larter et …
Characterization of ligands for the human T1R2 sweet taste receptor (obtention "Manfred Rothe Poster Award")
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…