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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 10129-10133 |
| Number of pages | 5 |
| Journal | Journal of agricultural and food chemistry |
| Volume | 54 |
| Issue number | 26 |
| DOIs | |
| State | Published - Dec 27 2006 |
Keywords
- Brazzein
- Docking
- Homology model
- Pentadiplandra brazzeana
- Sweetener
- Taste receptor
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