The crystal structure of gurmarin, a sweet taste-suppressing protein: Identification of the amino acid residues essential for inhibition - Université de Bourgogne Accéder directement au contenu
Article Dans Une Revue Chemical Senses Année : 2018

The crystal structure of gurmarin, a sweet taste-suppressing protein: Identification of the amino acid residues essential for inhibition

Résumé

Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning mutagenesis of the gurmarin molecule and a functional cell-based receptor assay, we confirmed that some single point mutations in these positions drastically affect sweet taste receptor inhibition by gurmarin.
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hal-02626068 , version 1 (26-05-2020)

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CC0 - Transfert dans le Domaine Public

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Maud Sigoillot, Anne Brockoff, Fabrice Neiers, Nicolas Poirier, Christine Belloir, et al.. The crystal structure of gurmarin, a sweet taste-suppressing protein: Identification of the amino acid residues essential for inhibition. Chemical Senses, 2018, 43 (8), pp.635-643. ⟨10.1093/chemse/bjy054⟩. ⟨hal-02626068⟩
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