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Appl. Chem. Vol. 74, No. 7, pp.
Pure and Applied Chemistry
Vol. 74, Issue 7
Homology-based model of the extracellular domain of the taste
D. Eric Walters
Department of Biochemistry and Molecular Biology, Chicago
Medical School, 3333 Green Bay Road, North Chicago, IL 60064, USA
Abstract: The extracellular ligand binding domain
of the sweet receptor T1R3 has been homology-modeled on the basis of
the crystal structure of the metabotropic glutamate receptor (mGluR1).
The region of the model that corresponds to the ligand binding site
of mGluR1 has numerous polar and charged side-chains, consistent with
expectations for a site that would respond to poly hydroxy compounds
such as mono- and disaccharides. Docking studies show that proposed
active conformations of the high-potency sweeteners neotame, superaspartame,
and SC-45647 could interact favorably in this binding site, forming
ion pairs or ionic hydrogen bonds with His-163, Glu-318, and His-407,
in addition to hydrophobic interactions with numerous nonpolar side-chains.
* A special topic issue on the
science of sweeteners.
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