Ligand recognition and allosteric modulation of the human MRGPRX1 receptor
The human MAS-related G protein–coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive alloster...
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| Veröffentlicht in: | Nature chemical biology 2023-04, Vol.19 (4), p.416-422 |
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| creator | Liu, Yongfeng Cao, Can Huang, Xi-Ping Gumpper, Ryan H. Rachman, Moira M. Shih, Sheng-Luen Krumm, Brian E. Zhang, Shicheng Shoichet, Brian K. Fay, Jonathan F. Roth, Bryan L. |
| description | The human MAS-related G protein–coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive allosteric modulator ML382 has been shown to effectively inhibit persistent pain, making MRGPRX1 a promising target for non-opioid pain treatment. However, the activation mechanism of MRGPRX1 is still largely unknown. Here we report three high-resolution cryogenic electron microscopy structures of MRGPRX1–Gαq in complex with BAM8-22 alone, with BAM8-22 and ML382 simultaneously as well as with a synthetic agonist compound-16. These structures reveal the agonist binding mode for MRGPRX1 and illuminate the structural requirements for positive allosteric modulation. Collectively, our findings provide a molecular understanding of the activation and allosteric modulation of the MRGPRX1 receptor, which could facilitate the structure-based design of non-opioid pain-relieving drugs.
The cryo-EM structures of MRGPRX1–Gq complexes are reported, which revealed the activation and allosteric modulation mechanism of human MRGPRX1 receptor, which may enable the structure-based identification of novel analgesics. |
| doi_str_mv | 10.1038/s41589-022-01173-6 |
| format | Article |
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The cryo-EM structures of MRGPRX1–Gq complexes are reported, which revealed the activation and allosteric modulation mechanism of human MRGPRX1 receptor, which may enable the structure-based identification of novel analgesics.</description><identifier>ISSN: 1552-4450</identifier><identifier>EISSN: 1552-4469</identifier><identifier>DOI: 10.1038/s41589-022-01173-6</identifier><identifier>PMID: 36302898</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/1647/2258 ; 631/80/86 ; 631/92/612/194 ; 631/92/613 ; Agonists ; Allosteric properties ; Allosteric Regulation ; Allosteric Site ; Analgesics ; Biochemical Engineering ; Biochemistry ; Bioorganic Chemistry ; Cell Biology ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Drug development ; Electron microscopy ; Humans ; Ligands ; Modulation ; Narcotics ; Opioid receptors ; Pain ; Pain perception ; Pruritus ; Receptors ; Receptors, G-Protein-Coupled - metabolism ; Sensory neurons</subject><ispartof>Nature chemical biology, 2023-04, Vol.19 (4), p.416-422</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2022. The Author(s), under exclusive licence to Springer Nature America, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-d497c1738fe629c6f80799ff85ff4b2b25b8c965b298966c8d1fba26dcb0974c3</citedby><cites>FETCH-LOGICAL-c375t-d497c1738fe629c6f80799ff85ff4b2b25b8c965b298966c8d1fba26dcb0974c3</cites><orcidid>0000-0002-8649-7892 ; 0000-0002-0561-6520 ; 0000-0001-6039-4767 ; 0000-0003-4017-741X ; 0000-0002-5245-443X ; 0000-0003-1822-2384 ; 0000-0002-6874-0529 ; 0000-0002-6098-7367</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36302898$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Yongfeng</creatorcontrib><creatorcontrib>Cao, Can</creatorcontrib><creatorcontrib>Huang, Xi-Ping</creatorcontrib><creatorcontrib>Gumpper, Ryan H.</creatorcontrib><creatorcontrib>Rachman, Moira M.</creatorcontrib><creatorcontrib>Shih, Sheng-Luen</creatorcontrib><creatorcontrib>Krumm, Brian E.</creatorcontrib><creatorcontrib>Zhang, Shicheng</creatorcontrib><creatorcontrib>Shoichet, Brian K.</creatorcontrib><creatorcontrib>Fay, Jonathan F.</creatorcontrib><creatorcontrib>Roth, Bryan L.</creatorcontrib><title>Ligand recognition and allosteric modulation of the human MRGPRX1 receptor</title><title>Nature chemical biology</title><addtitle>Nat Chem Biol</addtitle><addtitle>Nat Chem Biol</addtitle><description>The human MAS-related G protein–coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive allosteric modulator ML382 has been shown to effectively inhibit persistent pain, making MRGPRX1 a promising target for non-opioid pain treatment. However, the activation mechanism of MRGPRX1 is still largely unknown. Here we report three high-resolution cryogenic electron microscopy structures of MRGPRX1–Gαq in complex with BAM8-22 alone, with BAM8-22 and ML382 simultaneously as well as with a synthetic agonist compound-16. These structures reveal the agonist binding mode for MRGPRX1 and illuminate the structural requirements for positive allosteric modulation. Collectively, our findings provide a molecular understanding of the activation and allosteric modulation of the MRGPRX1 receptor, which could facilitate the structure-based design of non-opioid pain-relieving drugs.
The cryo-EM structures of MRGPRX1–Gq complexes are reported, which revealed the activation and allosteric modulation mechanism of human MRGPRX1 receptor, which may enable the structure-based identification of novel analgesics.</description><subject>631/1647/2258</subject><subject>631/80/86</subject><subject>631/92/612/194</subject><subject>631/92/613</subject><subject>Agonists</subject><subject>Allosteric properties</subject><subject>Allosteric Regulation</subject><subject>Allosteric Site</subject><subject>Analgesics</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Cell Biology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Drug development</subject><subject>Electron microscopy</subject><subject>Humans</subject><subject>Ligands</subject><subject>Modulation</subject><subject>Narcotics</subject><subject>Opioid receptors</subject><subject>Pain</subject><subject>Pain perception</subject><subject>Pruritus</subject><subject>Receptors</subject><subject>Receptors, G-Protein-Coupled - 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Academic</collection><jtitle>Nature chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Yongfeng</au><au>Cao, Can</au><au>Huang, Xi-Ping</au><au>Gumpper, Ryan H.</au><au>Rachman, Moira M.</au><au>Shih, Sheng-Luen</au><au>Krumm, Brian E.</au><au>Zhang, Shicheng</au><au>Shoichet, Brian K.</au><au>Fay, Jonathan F.</au><au>Roth, Bryan L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ligand recognition and allosteric modulation of the human MRGPRX1 receptor</atitle><jtitle>Nature chemical biology</jtitle><stitle>Nat Chem Biol</stitle><addtitle>Nat Chem Biol</addtitle><date>2023-04-01</date><risdate>2023</risdate><volume>19</volume><issue>4</issue><spage>416</spage><epage>422</epage><pages>416-422</pages><issn>1552-4450</issn><eissn>1552-4469</eissn><abstract>The human MAS-related G protein–coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive allosteric modulator ML382 has been shown to effectively inhibit persistent pain, making MRGPRX1 a promising target for non-opioid pain treatment. However, the activation mechanism of MRGPRX1 is still largely unknown. Here we report three high-resolution cryogenic electron microscopy structures of MRGPRX1–Gαq in complex with BAM8-22 alone, with BAM8-22 and ML382 simultaneously as well as with a synthetic agonist compound-16. These structures reveal the agonist binding mode for MRGPRX1 and illuminate the structural requirements for positive allosteric modulation. Collectively, our findings provide a molecular understanding of the activation and allosteric modulation of the MRGPRX1 receptor, which could facilitate the structure-based design of non-opioid pain-relieving drugs.
The cryo-EM structures of MRGPRX1–Gq complexes are reported, which revealed the activation and allosteric modulation mechanism of human MRGPRX1 receptor, which may enable the structure-based identification of novel analgesics.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>36302898</pmid><doi>10.1038/s41589-022-01173-6</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-8649-7892</orcidid><orcidid>https://orcid.org/0000-0002-0561-6520</orcidid><orcidid>https://orcid.org/0000-0001-6039-4767</orcidid><orcidid>https://orcid.org/0000-0003-4017-741X</orcidid><orcidid>https://orcid.org/0000-0002-5245-443X</orcidid><orcidid>https://orcid.org/0000-0003-1822-2384</orcidid><orcidid>https://orcid.org/0000-0002-6874-0529</orcidid><orcidid>https://orcid.org/0000-0002-6098-7367</orcidid></addata></record> |
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| subjects | 631/1647/2258 631/80/86 631/92/612/194 631/92/613 Agonists Allosteric properties Allosteric Regulation Allosteric Site Analgesics Biochemical Engineering Biochemistry Bioorganic Chemistry Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Drug development Electron microscopy Humans Ligands Modulation Narcotics Opioid receptors Pain Pain perception Pruritus Receptors Receptors, G-Protein-Coupled - metabolism Sensory neurons |
| title | Ligand recognition and allosteric modulation of the human MRGPRX1 receptor |
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