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Interactions of the sweet protein brazzein with the sweet taste receptor
D Eric Walters1, Göran Hellekant
1Department of Biochemistry and Molecular Biology, The Chicago Medical School, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Road, North Chicago, Illinois 60064, USA. Eric.Walters@RosalindFranklin.edu
Abstract:
Brazzein is a small, potently sweet protein. Homology modeling has been used to construct a model of the ligand-binding domain of the sweet taste receptor, and low-resolution docking has been used to identify potential modes of brazzein-receptor binding. Published brazzein mutation-taste data were then used to select one of these as the most likely brazzein-receptor binding orientation. This orientation places brazzein in contact primarily with the T1R2 subunit of the receptor, and it accounts for 21 of the 23 mutation results examined.
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