Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor
Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor
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DOI：
10.1016/s0014-5793(02)03155-1
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发表时间：
2002-08-28
期刊：
影响因子：
3.5
通讯作者：
Temussi, PA
中科院分区：
文献类型：
--
作者：
Temussi, PA
甜味蛋白与结合小分子甜味剂的同一受体T1R2-T1R3 G蛋白偶联受体相互作用，但蛋白质表面负责生物活性的关键基团尚未确定。我认为，与小配体相反，甜蛋白不会与谷氨酸样囊袋结合，而是通过与二级结合位点结合来稳定T1R2-T1R3受体的游离型II。将brazzein、monellin和thaumatin与T1R2-T1R3甜味受体模型对接表明，最有可能的络合物确实可以稳定该受体的活性形式。(C)2002年欧洲生化学会联合会。爱思唯尔科学公司出版。版权所有。
Sweet tasting proteins interact with the same receptor that binds small molecular weight sweeteners, the T1R2-T1R3 G-protein coupled receptor, but the key groups on the protein surface responsible for the biological activity have not yet been identified. I propose that sweet proteins, contrary to small ligands, do not bind to the 'glutamate-like' pocket but stabilize the free form II of the T1R2-T1R3 receptor by attachment to a secondary binding site. Docking of brazzein, monellin and thaumatin with a model of the T1R2-T1R3 sweet taste receptor shows that the most likely complexes can indeed stabilize the active form of the receptor. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.