I  U  P  A  C




News & Notices

Organizations & People

Standing Committees




. . CI
. . PAC
. . Macro. Symp.

. . Books
. . Solubility Data



Links of Interest

Search the Site

Home Page


Pure Appl. Chem. Vol. 74, No. 7, pp. 1117-1123 (2002)

Pure and Applied Chemistry

Vol. 74, Issue 7

Homology-based model of the extracellular domain of the taste receptor T1R3*

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.

Contacct information: E-mail: [email protected]** Corresponding author.

Page last modified 19 August 2002.
Copyright © 2002 International Union of Pure and Applied Chemistry.
Questions or comments about IUPAC, please contact, the Secretariat.
Questions regarding the website, please contact web manager.