Protein-protein docking studies on the sweet protein (neoculin) and the human sweet taste receptors T1R2 and T1R3

• Main Authors: Ahmad Khairudin, Nurul Bahiyah, Yousif, Ragheed Hussam
• Format: Conference or Workshop Item
• Published: 2015
• Subjects: QP Physiology
• Online Access: http://eprints.utm.my/id/eprint/61218/; http://scmsm2015.utem.edu.my/
• Institution: Universiti Teknologi Malaysia

Neoculin is a sweet protein capable to alter the sour taste into sweet taste, it is 500 times sweeter than the ordinary sugar. This protein has been discovered in Malaysia under the name of Curculin. There are a number of experimental studies that have been conducted on neoculin but none of the studies focuses on molecular level, in order to understand how the protein interacts with the human sweet taste receptors T1R2 and T1R3. Therefore, in this work, a protein-protein docking study was performed between neoculin and the human sweet taste receptor T1R2 and T1R3. The docking results showed residues that might be important for binding the neoculin with the human sweet taste receptors, particularly T1R3 at the amino terminal domain (ATD). In addition, the current results showed that His11, which is important for the taste modifying ability does not bind directly to the human sweet taste receptors.