The anatomy of mammalian sweet taste receptors
ABSTRACT All sweet‐tasting compounds are detected by a single G‐protein coupled receptor (GPCR), the heterodimer T1R2‐T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate r...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2017-02, Vol.85 (2), p.332-341 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Chéron, Jean‐Baptiste Golebiowski, Jérôme Antonczak, Serge Fiorucci, Sébastien |
| description | ABSTRACT
All sweet‐tasting compounds are detected by a single G‐protein coupled receptor (GPCR), the heterodimer T1R2‐T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate receptor (mGluR) 1 and 5 provide a significant step forward for understanding structure‐function relationships within this family. In this article, we recapitulate more than 600 single point site‐directed mutations and available structural data to obtain a critical alignment of the sweet taste receptor sequences with respect to other class C GPCRs. Using this alignment, a homology 3D‐model of the human sweet taste receptor is built and analyzed to dissect out the role of key residues involved in ligand binding and those responsible for receptor activation. Proteins 2017; 85:332–341. © 2016 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/prot.25228 |
| format | Article |
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All sweet‐tasting compounds are detected by a single G‐protein coupled receptor (GPCR), the heterodimer T1R2‐T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate receptor (mGluR) 1 and 5 provide a significant step forward for understanding structure‐function relationships within this family. In this article, we recapitulate more than 600 single point site‐directed mutations and available structural data to obtain a critical alignment of the sweet taste receptor sequences with respect to other class C GPCRs. Using this alignment, a homology 3D‐model of the human sweet taste receptor is built and analyzed to dissect out the role of key residues involved in ligand binding and those responsible for receptor activation. Proteins 2017; 85:332–341. © 2016 Wiley Periodicals, Inc.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/prot.25228</identifier><identifier>PMID: 27936499</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Amino Acid Sequence ; Anatomy ; Binding Sites ; Bioinformatics ; Chemical Sciences ; chemical senses ; Cheminformatics ; class C ; Computer Science ; G protein-coupled receptors ; Gene Expression ; Glutamic acid receptors (metabotropic) ; GPCR ; Homology ; Humans ; Ligands ; Models, Molecular ; or physical chemistry ; Point Mutation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Receptor mechanisms ; Receptor, Metabotropic Glutamate 5 - chemistry ; Receptor, Metabotropic Glutamate 5 - genetics ; Receptors, G-Protein-Coupled - chemistry ; Receptors, G-Protein-Coupled - genetics ; Receptors, Metabotropic Glutamate - chemistry ; Receptors, Metabotropic Glutamate - genetics ; Sequence Alignment ; Structural Homology, Protein ; Structure-function relationships ; Sweet taste ; Sweetening Agents - chemistry ; T1R ; Taste ; Taste - physiology ; Taste receptors ; Theoretical and ; Tongue</subject><ispartof>Proteins, structure, function, and bioinformatics, 2017-02, Vol.85 (2), p.332-341</ispartof><rights>2016 Wiley Periodicals, Inc.</rights><rights>2017 Wiley Periodicals, Inc.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4838-1b7b6dae528c42a49ff63ec891eaf08e1c108d79c2b5d9480eda636d5e7610dd3</citedby><orcidid>0000-0003-2245-0478 ; 0000-0002-3675-1952</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fprot.25228$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fprot.25228$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,777,781,882,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27936499$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02545213$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Chéron, Jean‐Baptiste</creatorcontrib><creatorcontrib>Golebiowski, Jérôme</creatorcontrib><creatorcontrib>Antonczak, Serge</creatorcontrib><creatorcontrib>Fiorucci, Sébastien</creatorcontrib><title>The anatomy of mammalian sweet taste receptors</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>ABSTRACT
All sweet‐tasting compounds are detected by a single G‐protein coupled receptor (GPCR), the heterodimer T1R2‐T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate receptor (mGluR) 1 and 5 provide a significant step forward for understanding structure‐function relationships within this family. In this article, we recapitulate more than 600 single point site‐directed mutations and available structural data to obtain a critical alignment of the sweet taste receptor sequences with respect to other class C GPCRs. Using this alignment, a homology 3D‐model of the human sweet taste receptor is built and analyzed to dissect out the role of key residues involved in ligand binding and those responsible for receptor activation. Proteins 2017; 85:332–341. © 2016 Wiley Periodicals, Inc.</description><subject>Amino Acid Sequence</subject><subject>Anatomy</subject><subject>Binding Sites</subject><subject>Bioinformatics</subject><subject>Chemical Sciences</subject><subject>chemical senses</subject><subject>Cheminformatics</subject><subject>class C</subject><subject>Computer Science</subject><subject>G protein-coupled receptors</subject><subject>Gene Expression</subject><subject>Glutamic acid receptors (metabotropic)</subject><subject>GPCR</subject><subject>Homology</subject><subject>Humans</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>or physical chemistry</subject><subject>Point Mutation</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Receptor mechanisms</subject><subject>Receptor, Metabotropic Glutamate 5 - chemistry</subject><subject>Receptor, Metabotropic Glutamate 5 - genetics</subject><subject>Receptors, G-Protein-Coupled - chemistry</subject><subject>Receptors, G-Protein-Coupled - genetics</subject><subject>Receptors, Metabotropic Glutamate - chemistry</subject><subject>Receptors, Metabotropic Glutamate - genetics</subject><subject>Sequence Alignment</subject><subject>Structural Homology, Protein</subject><subject>Structure-function relationships</subject><subject>Sweet taste</subject><subject>Sweetening Agents - chemistry</subject><subject>T1R</subject><subject>Taste</subject><subject>Taste - physiology</subject><subject>Taste receptors</subject><subject>Theoretical and</subject><subject>Tongue</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0U1Lw0AQBuBFFFurF3-ABLzoIXVmN_t1lOIXFCpSz8s2mdCUpKnZVOm_N7XVgxc9zTL7MDDzMnaOMEQAfrNq6nbIJefmgPURrI4BRXLI-mCMjoU0ssdOQlgAgLJCHbMe111NrO2z4XROkV_6tq42UZ1Hla8qXxZ-GYUPojZqfWgpaiilVVs34ZQd5b4MdLavA_Z6fzcdPcbjycPT6HYcp4kRJsaZnqnMk-QmTbhPbJ4rQamxSD4HQ5gimEzblM9kZhMDlHklVCZJK4QsEwN2vZs796VbNUXlm42rfeEeb8du2wMuE8lRvGNnr3a2u8PbmkLrqiKkVJZ-SfU6ODTKiISjFP-gkitpOZcdvfxFF_W6WXZLd8pqJYXEP5QChRq06dTFXq1nFWU_C33H0AHcgY-ipM3PP4LbBuy2AbuvgN3zy2T69RKfSZCUig</recordid><startdate>201702</startdate><enddate>201702</enddate><creator>Chéron, Jean‐Baptiste</creator><creator>Golebiowski, Jérôme</creator><creator>Antonczak, Serge</creator><creator>Fiorucci, Sébastien</creator><general>Wiley Subscription Services, Inc</general><general>Wiley</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-2245-0478</orcidid><orcidid>https://orcid.org/0000-0002-3675-1952</orcidid></search><sort><creationdate>201702</creationdate><title>The anatomy of mammalian sweet taste receptors</title><author>Chéron, Jean‐Baptiste ; Golebiowski, Jérôme ; Antonczak, Serge ; Fiorucci, Sébastien</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4838-1b7b6dae528c42a49ff63ec891eaf08e1c108d79c2b5d9480eda636d5e7610dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence</topic><topic>Anatomy</topic><topic>Binding Sites</topic><topic>Bioinformatics</topic><topic>Chemical Sciences</topic><topic>chemical senses</topic><topic>Cheminformatics</topic><topic>class C</topic><topic>Computer Science</topic><topic>G protein-coupled receptors</topic><topic>Gene Expression</topic><topic>Glutamic acid receptors (metabotropic)</topic><topic>GPCR</topic><topic>Homology</topic><topic>Humans</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>or physical chemistry</topic><topic>Point Mutation</topic><topic>Protein Binding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Secondary</topic><topic>Receptor mechanisms</topic><topic>Receptor, Metabotropic Glutamate 5 - chemistry</topic><topic>Receptor, Metabotropic Glutamate 5 - genetics</topic><topic>Receptors, G-Protein-Coupled - chemistry</topic><topic>Receptors, G-Protein-Coupled - genetics</topic><topic>Receptors, Metabotropic Glutamate - chemistry</topic><topic>Receptors, Metabotropic Glutamate - genetics</topic><topic>Sequence Alignment</topic><topic>Structural Homology, Protein</topic><topic>Structure-function relationships</topic><topic>Sweet taste</topic><topic>Sweetening Agents - chemistry</topic><topic>T1R</topic><topic>Taste</topic><topic>Taste - physiology</topic><topic>Taste receptors</topic><topic>Theoretical and</topic><topic>Tongue</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chéron, Jean‐Baptiste</creatorcontrib><creatorcontrib>Golebiowski, Jérôme</creatorcontrib><creatorcontrib>Antonczak, Serge</creatorcontrib><creatorcontrib>Fiorucci, Sébastien</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chéron, Jean‐Baptiste</au><au>Golebiowski, Jérôme</au><au>Antonczak, Serge</au><au>Fiorucci, Sébastien</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The anatomy of mammalian sweet taste receptors</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2017-02</date><risdate>2017</risdate><volume>85</volume><issue>2</issue><spage>332</spage><epage>341</epage><pages>332-341</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>ABSTRACT
All sweet‐tasting compounds are detected by a single G‐protein coupled receptor (GPCR), the heterodimer T1R2‐T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate receptor (mGluR) 1 and 5 provide a significant step forward for understanding structure‐function relationships within this family. In this article, we recapitulate more than 600 single point site‐directed mutations and available structural data to obtain a critical alignment of the sweet taste receptor sequences with respect to other class C GPCRs. Using this alignment, a homology 3D‐model of the human sweet taste receptor is built and analyzed to dissect out the role of key residues involved in ligand binding and those responsible for receptor activation. Proteins 2017; 85:332–341. © 2016 Wiley Periodicals, Inc.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>27936499</pmid><doi>10.1002/prot.25228</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-2245-0478</orcidid><orcidid>https://orcid.org/0000-0002-3675-1952</orcidid></addata></record> |
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| ispartof | Proteins, structure, function, and bioinformatics, 2017-02, Vol.85 (2), p.332-341 |
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| subjects | Amino Acid Sequence Anatomy Binding Sites Bioinformatics Chemical Sciences chemical senses Cheminformatics class C Computer Science G protein-coupled receptors Gene Expression Glutamic acid receptors (metabotropic) GPCR Homology Humans Ligands Models, Molecular or physical chemistry Point Mutation Protein Binding Protein Interaction Domains and Motifs Protein Multimerization Protein Structure, Secondary Receptor mechanisms Receptor, Metabotropic Glutamate 5 - chemistry Receptor, Metabotropic Glutamate 5 - genetics Receptors, G-Protein-Coupled - chemistry Receptors, G-Protein-Coupled - genetics Receptors, Metabotropic Glutamate - chemistry Receptors, Metabotropic Glutamate - genetics Sequence Alignment Structural Homology, Protein Structure-function relationships Sweet taste Sweetening Agents - chemistry T1R Taste Taste - physiology Taste receptors Theoretical and Tongue |
| title | The anatomy of mammalian sweet taste receptors |
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