title: Interactions of the sweet protein brazzein with the sweet taste receptor.
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.
authors.affiliation: Department 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
authors.forename: D Eric
authors.initials: DE
authors.lastname: Walters
authors.forename: Göran
authors.initials: G
authors.lastname: Hellekant
mesh_terms: D001665:Binding Sites; D006801:Humans; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D043562:Receptors, G-Protein-Coupled; C090521:brazzein protein, Pentadiplandra brazzeana; C431926:taste receptors, type 1