Binding of glutamate to the umami receptor.
The umami taste receptor is a heterodimer composed of two members of the T1R taste receptor family: T1R1 and T1R3. It detects glutamate in humans, and is a more general amino acid detector in other species. We have constructed homology models of the ligand binding domains of the human umami receptor (based on crystallographic structures of the metabotropic glutamate receptor of the central nervous system). We have carried out molecular dynamics simulations of the ligand binding domains, and we find that the likely conformation is that T1R1 receptor protein exists in the closed conformation, and T1R3 receptor in the open conformation in the heterodimer. Further, we have identified the important binding interactions and have made an estimate of the relative free energies associated with the two glutamate binding sites.
Universidad Politécnica de Cartagena, Bioinformatic and Macromolecules Group, Aulario II, Campus de Alfonso XIII, 30203 Cartagena, Murcia, Spain.
J J
JJ
López Cascales
S D
SD
Oliveira Costa
Bert L
BL
de Groot
D Eric
DE
Walters
D001665:Binding Sites; D018698:Glutamic Acid / Q000737:chemistry*; D006801:Humans; D017705:Lignans; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
D017705:Lignans; D043562:Receptors, G-Protein-Coupled; C431926:taste receptors, type 1; D018698:Glutamic Acid