Chemical Senses Vol. 30 No. suppl 1 © Oxford University
Press 2005; all rights reserved
Molecular Mechanisms of Sweet Receptor Function
1 Physiology and Biophysics, Mount Sinai School of Medicine 2 Howard Hughes Medical Institute, Mount Sinai School of Medicine
Correspondence to be sent to: Marianna Max, e-mail: max@inka.mssm.edu
Key words: brazzein, GPCR, sweet-finger, T1R2, T1R3
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Introduction |
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The T1R taste receptors, like other type 3 G-protein-coupled receptors (GPCRs), have a large amino terminal extracellular domain. Type 3 GPCRs typically function as dimers, but each monomer can independently bind ligand. Based on studies with the metabotropic glutamate receptors (mGluRs) the site for ligand binding in type 3 GPCRs is thought to be in a shell-like cleft formed by two lobes within the extracellular domain. Occupation of the binding cleft and binding to both of the lobes allows the ‘shells’ to close and stabilizes the active conformation of the receptor (Kunishima et al., 2000
;
Jingami et al., 2003).
T1R2 + T1R3 monomers form a heterodimeric receptor that is responsive to
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Results and discussion |
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The ‘sweet finger’ model
Single mutations in hT1R2 alter ligand-induced activity
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Methods |
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Homology modeling
Construction of T1R mutants, heterologous expression and functional assays
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