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Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor
Glucose-dependent insulinotropic polypeptide (GIP) is a peptide hormone that exerts crucial metabolic functions by binding and activating its cognate receptor, GIPR. As an important therapeutic target, GIPR has been subjected to intensive structural studies without success. Here, we report the cryo-...
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| Published in: | eLife 2021-07, Vol.10 |
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| creator | Zhao, Fenghui Zhang, Chao Zhou, Qingtong Hang, Kaini Zou, Xinyu Chen, Yan Wu, Fan Rao, Qidi Dai, Antao Yin, Wanchao Shen, Dan-Dan Zhang, Yan Xia, Tian Stevens, Raymond C Xu, H Eric Yang, Dehua Zhao, Lihua Wang, Ming-Wei |
| description | Glucose-dependent insulinotropic polypeptide (GIP) is a peptide hormone that exerts crucial metabolic functions by binding and activating its cognate receptor, GIPR. As an important therapeutic target, GIPR has been subjected to intensive structural studies without success. Here, we report the cryo-EM structure of the human GIPR in complex with GIP and a G
heterotrimer at a global resolution of 2.9 Å. GIP adopts a single straight helix with its N terminus dipped into the receptor transmembrane domain (TMD), while the C terminus is closely associated with the extracellular domain and extracellular loop 1. GIPR employs conserved residues in the lower half of the TMD pocket to recognize the common segments shared by GIP homologous peptides, while uses non-conserved residues in the upper half of the TMD pocket to interact with residues specific for GIP. These results provide a structural framework of hormone recognition and GIPR activation. |
| doi_str_mv | 10.7554/eLife.68719 |
| format | article |
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heterotrimer at a global resolution of 2.9 Å. GIP adopts a single straight helix with its N terminus dipped into the receptor transmembrane domain (TMD), while the C terminus is closely associated with the extracellular domain and extracellular loop 1. GIPR employs conserved residues in the lower half of the TMD pocket to recognize the common segments shared by GIP homologous peptides, while uses non-conserved residues in the upper half of the TMD pocket to interact with residues specific for GIP. These results provide a structural framework of hormone recognition and GIPR activation.</description><identifier>ISSN: 2050-084X</identifier><identifier>EISSN: 2050-084X</identifier><identifier>DOI: 10.7554/eLife.68719</identifier><identifier>PMID: 34254582</identifier><language>eng</language><publisher>England: eLife Sciences Publications Ltd</publisher><subject>Amino acids ; Animals ; C-Terminus ; Cell Line ; Chromatography ; cryo-electron microscopy ; Cryoelectron Microscopy ; Data collection ; Fatty acids ; G protein-coupled receptor ; Gastric Inhibitory Polypeptide - chemistry ; Gastric Inhibitory Polypeptide - metabolism ; GIP protein ; Glucagon ; Glucose ; glucose-dependent insulinotropic polypeptide receptor ; Humans ; ligand recognition ; Ligands ; Lipids ; Molecular Dynamics Simulation ; Mutation ; Polypeptides ; Protein Conformation ; Protein Conformation, alpha-Helical ; Protein Domains ; Proteins ; Receptors, Gastrointestinal Hormone - chemistry ; Receptors, Gastrointestinal Hormone - metabolism ; Structural Biology and Molecular Biophysics</subject><ispartof>eLife, 2021-07, Vol.10</ispartof><rights>2021, Zhao et al.</rights><rights>2021, Zhao et al. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021, Zhao et al 2021 Zhao et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-418e81379b71b6aa774c19d5ceb5a386bddfffd1d355673684ae0ce20ac524a63</citedby><cites>FETCH-LOGICAL-c405t-418e81379b71b6aa774c19d5ceb5a386bddfffd1d355673684ae0ce20ac524a63</cites><orcidid>0000-0001-8124-3079 ; 0000-0003-3028-3243 ; 0000-0001-6550-9017</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2595211576/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2595211576?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25732,27903,27904,36991,36992,44569,53770,53772,74873</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34254582$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Fenghui</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Zhou, Qingtong</creatorcontrib><creatorcontrib>Hang, Kaini</creatorcontrib><creatorcontrib>Zou, Xinyu</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><creatorcontrib>Wu, Fan</creatorcontrib><creatorcontrib>Rao, Qidi</creatorcontrib><creatorcontrib>Dai, Antao</creatorcontrib><creatorcontrib>Yin, Wanchao</creatorcontrib><creatorcontrib>Shen, Dan-Dan</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Xia, Tian</creatorcontrib><creatorcontrib>Stevens, Raymond C</creatorcontrib><creatorcontrib>Xu, H Eric</creatorcontrib><creatorcontrib>Yang, Dehua</creatorcontrib><creatorcontrib>Zhao, Lihua</creatorcontrib><creatorcontrib>Wang, Ming-Wei</creatorcontrib><title>Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor</title><title>eLife</title><addtitle>Elife</addtitle><description>Glucose-dependent insulinotropic polypeptide (GIP) is a peptide hormone that exerts crucial metabolic functions by binding and activating its cognate receptor, GIPR. As an important therapeutic target, GIPR has been subjected to intensive structural studies without success. Here, we report the cryo-EM structure of the human GIPR in complex with GIP and a G
heterotrimer at a global resolution of 2.9 Å. GIP adopts a single straight helix with its N terminus dipped into the receptor transmembrane domain (TMD), while the C terminus is closely associated with the extracellular domain and extracellular loop 1. GIPR employs conserved residues in the lower half of the TMD pocket to recognize the common segments shared by GIP homologous peptides, while uses non-conserved residues in the upper half of the TMD pocket to interact with residues specific for GIP. These results provide a structural framework of hormone recognition and GIPR activation.</description><subject>Amino acids</subject><subject>Animals</subject><subject>C-Terminus</subject><subject>Cell Line</subject><subject>Chromatography</subject><subject>cryo-electron microscopy</subject><subject>Cryoelectron Microscopy</subject><subject>Data collection</subject><subject>Fatty acids</subject><subject>G protein-coupled receptor</subject><subject>Gastric Inhibitory Polypeptide - chemistry</subject><subject>Gastric Inhibitory Polypeptide - metabolism</subject><subject>GIP protein</subject><subject>Glucagon</subject><subject>Glucose</subject><subject>glucose-dependent insulinotropic polypeptide receptor</subject><subject>Humans</subject><subject>ligand recognition</subject><subject>Ligands</subject><subject>Lipids</subject><subject>Molecular Dynamics Simulation</subject><subject>Mutation</subject><subject>Polypeptides</subject><subject>Protein Conformation</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Domains</subject><subject>Proteins</subject><subject>Receptors, Gastrointestinal Hormone - 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chemistry</topic><topic>Gastric Inhibitory Polypeptide - metabolism</topic><topic>GIP protein</topic><topic>Glucagon</topic><topic>Glucose</topic><topic>glucose-dependent insulinotropic polypeptide receptor</topic><topic>Humans</topic><topic>ligand recognition</topic><topic>Ligands</topic><topic>Lipids</topic><topic>Molecular Dynamics Simulation</topic><topic>Mutation</topic><topic>Polypeptides</topic><topic>Protein Conformation</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Domains</topic><topic>Proteins</topic><topic>Receptors, Gastrointestinal Hormone - chemistry</topic><topic>Receptors, Gastrointestinal Hormone - metabolism</topic><topic>Structural Biology and Molecular Biophysics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Fenghui</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Zhou, Qingtong</creatorcontrib><creatorcontrib>Hang, Kaini</creatorcontrib><creatorcontrib>Zou, Xinyu</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><creatorcontrib>Wu, Fan</creatorcontrib><creatorcontrib>Rao, Qidi</creatorcontrib><creatorcontrib>Dai, Antao</creatorcontrib><creatorcontrib>Yin, Wanchao</creatorcontrib><creatorcontrib>Shen, Dan-Dan</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Xia, Tian</creatorcontrib><creatorcontrib>Stevens, Raymond C</creatorcontrib><creatorcontrib>Xu, H Eric</creatorcontrib><creatorcontrib>Yang, Dehua</creatorcontrib><creatorcontrib>Zhao, Lihua</creatorcontrib><creatorcontrib>Wang, Ming-Wei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>ProQuest Biological Science Journals</collection><collection>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>eLife</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Fenghui</au><au>Zhang, Chao</au><au>Zhou, Qingtong</au><au>Hang, Kaini</au><au>Zou, Xinyu</au><au>Chen, Yan</au><au>Wu, Fan</au><au>Rao, Qidi</au><au>Dai, Antao</au><au>Yin, Wanchao</au><au>Shen, Dan-Dan</au><au>Zhang, Yan</au><au>Xia, Tian</au><au>Stevens, Raymond C</au><au>Xu, H Eric</au><au>Yang, Dehua</au><au>Zhao, Lihua</au><au>Wang, Ming-Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor</atitle><jtitle>eLife</jtitle><addtitle>Elife</addtitle><date>2021-07-13</date><risdate>2021</risdate><volume>10</volume><issn>2050-084X</issn><eissn>2050-084X</eissn><abstract>Glucose-dependent insulinotropic polypeptide (GIP) is a peptide hormone that exerts crucial metabolic functions by binding and activating its cognate receptor, GIPR. As an important therapeutic target, GIPR has been subjected to intensive structural studies without success. Here, we report the cryo-EM structure of the human GIPR in complex with GIP and a G
heterotrimer at a global resolution of 2.9 Å. GIP adopts a single straight helix with its N terminus dipped into the receptor transmembrane domain (TMD), while the C terminus is closely associated with the extracellular domain and extracellular loop 1. GIPR employs conserved residues in the lower half of the TMD pocket to recognize the common segments shared by GIP homologous peptides, while uses non-conserved residues in the upper half of the TMD pocket to interact with residues specific for GIP. These results provide a structural framework of hormone recognition and GIPR activation.</abstract><cop>England</cop><pub>eLife Sciences Publications Ltd</pub><pmid>34254582</pmid><doi>10.7554/eLife.68719</doi><orcidid>https://orcid.org/0000-0001-8124-3079</orcidid><orcidid>https://orcid.org/0000-0003-3028-3243</orcidid><orcidid>https://orcid.org/0000-0001-6550-9017</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Animals C-Terminus Cell Line Chromatography cryo-electron microscopy Cryoelectron Microscopy Data collection Fatty acids G protein-coupled receptor Gastric Inhibitory Polypeptide - chemistry Gastric Inhibitory Polypeptide - metabolism GIP protein Glucagon Glucose glucose-dependent insulinotropic polypeptide receptor Humans ligand recognition Ligands Lipids Molecular Dynamics Simulation Mutation Polypeptides Protein Conformation Protein Conformation, alpha-Helical Protein Domains Proteins Receptors, Gastrointestinal Hormone - chemistry Receptors, Gastrointestinal Hormone - metabolism Structural Biology and Molecular Biophysics |
| title | Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor |
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