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- Title
The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition.
- Authors
Sigoillot, Maud; Brockhoff, Anne; Neiers, Fabrice; Poirier, Nicolas; Belloir, Christine; Legrand, Pierre; Charron, Christophe; Roblin, Pierre; Meyerhof, Wolfgang; Briand, Loïc
- Abstract
Gurmarin is a highly specific sweet taste–suppressing protein in rodents that is isolated from the Indian plant Gymnema sylvestre. Gurmarin consists of 35 amino acid residues containing 3 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 nuclear magnetic resonance 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.
- Subjects
CRYSTAL structure; AMINO acids; CYSTINE; NUCLEAR magnetic resonance; LABORATORY animals
- Publication
Chemical Senses, 2018, Vol 43, Issue 8, p635
- ISSN
0379-864X
- Publication type
Article
- DOI
10.1093/chemse/bjy054