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Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16
G-protein-coupled receptors mediate the senses of taste, smell, and vision in mammals. Humans recognize thousands of compounds as bitter, and this response is mediated by the hTAS2R family, which is one of the G-protein-coupled receptors composed of only 25 receptors. However, structural information...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2934701/ https://www.ncbi.nlm.nih.gov/pubmed/20605788 http://dx.doi.org/10.1074/jbc.M110.144444 |
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author | Sakurai, Takanobu Misaka, Takumi Ishiguro, Masaji Masuda, Katsuyoshi Sugawara, Taishi Ito, Keisuke Kobayashi, Takuya Matsuo, Shinji Ishimaru, Yoshiro Asakura, Tomiko Abe, Keiko |
author_facet | Sakurai, Takanobu Misaka, Takumi Ishiguro, Masaji Masuda, Katsuyoshi Sugawara, Taishi Ito, Keisuke Kobayashi, Takuya Matsuo, Shinji Ishimaru, Yoshiro Asakura, Tomiko Abe, Keiko |
author_sort | Sakurai, Takanobu |
collection | PubMed |
description | G-protein-coupled receptors mediate the senses of taste, smell, and vision in mammals. Humans recognize thousands of compounds as bitter, and this response is mediated by the hTAS2R family, which is one of the G-protein-coupled receptors composed of only 25 receptors. However, structural information on these receptors is limited. To address the molecular basis of bitter tastant discrimination by the hTAS2Rs, we performed ligand docking simulation and functional analysis using a series of point mutants of hTAS2R16 to identify its binding sites. The docking simulation predicted two candidate binding structures for a salicin-hTAS2R16 complex, and at least seven amino acid residues in transmembrane 3 (TM3), TM5, and TM6 were shown to be involved in ligand recognition. We also identified the probable salicin-hTAS2R16 binding mode using a mutated receptor experiment. This study characterizes the molecular interaction between hTAS2R16 and β-d-glucopyranoside and will also facilitate rational design of bitter blockers. |
format | Text |
id | pubmed-2934701 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29347012010-09-13 Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 Sakurai, Takanobu Misaka, Takumi Ishiguro, Masaji Masuda, Katsuyoshi Sugawara, Taishi Ito, Keisuke Kobayashi, Takuya Matsuo, Shinji Ishimaru, Yoshiro Asakura, Tomiko Abe, Keiko J Biol Chem Signal Transduction G-protein-coupled receptors mediate the senses of taste, smell, and vision in mammals. Humans recognize thousands of compounds as bitter, and this response is mediated by the hTAS2R family, which is one of the G-protein-coupled receptors composed of only 25 receptors. However, structural information on these receptors is limited. To address the molecular basis of bitter tastant discrimination by the hTAS2Rs, we performed ligand docking simulation and functional analysis using a series of point mutants of hTAS2R16 to identify its binding sites. The docking simulation predicted two candidate binding structures for a salicin-hTAS2R16 complex, and at least seven amino acid residues in transmembrane 3 (TM3), TM5, and TM6 were shown to be involved in ligand recognition. We also identified the probable salicin-hTAS2R16 binding mode using a mutated receptor experiment. This study characterizes the molecular interaction between hTAS2R16 and β-d-glucopyranoside and will also facilitate rational design of bitter blockers. American Society for Biochemistry and Molecular Biology 2010-09-03 2010-07-06 /pmc/articles/PMC2934701/ /pubmed/20605788 http://dx.doi.org/10.1074/jbc.M110.144444 Text en © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Signal Transduction Sakurai, Takanobu Misaka, Takumi Ishiguro, Masaji Masuda, Katsuyoshi Sugawara, Taishi Ito, Keisuke Kobayashi, Takuya Matsuo, Shinji Ishimaru, Yoshiro Asakura, Tomiko Abe, Keiko Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title | Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title_full | Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title_fullStr | Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title_full_unstemmed | Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title_short | Characterization of the β-d-Glucopyranoside Binding Site of the Human Bitter Taste Receptor hTAS2R16 |
title_sort | characterization of the β-d-glucopyranoside binding site of the human bitter taste receptor htas2r16 |
topic | Signal Transduction |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2934701/ https://www.ncbi.nlm.nih.gov/pubmed/20605788 http://dx.doi.org/10.1074/jbc.M110.144444 |
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