Demet Arac-Ozkan, Gabriela Aust, Tom I. Bonner, Heike Cappallo-Obermann, Caroline Formstone, Jörg Hamann, Breanne Harty, Henrike Heyne, Christiane Kirchhoff, Barbara Knapp, Arunkumar Krishnan, Tobias Langenhan, Diana Le Duc, Hsi-Hsien Lin, David C. Martinelli, Kelly Monk, Xianhua Piao, Simone Prömel, Torsten Schöneberg, Helgi Schiöth, Kathleen Singer, Martin Stacey, Yuri Ushkaryov, Uwe Wolfrum, Lei Xu
{"title":"GtoPdb v.2023.1中粘附级gpcr","authors":"Demet Arac-Ozkan, Gabriela Aust, Tom I. Bonner, Heike Cappallo-Obermann, Caroline Formstone, Jörg Hamann, Breanne Harty, Henrike Heyne, Christiane Kirchhoff, Barbara Knapp, Arunkumar Krishnan, Tobias Langenhan, Diana Le Duc, Hsi-Hsien Lin, David C. Martinelli, Kelly Monk, Xianhua Piao, Simone Prömel, Torsten Schöneberg, Helgi Schiöth, Kathleen Singer, Martin Stacey, Yuri Ushkaryov, Uwe Wolfrum, Lei Xu","doi":"10.2218/gtopdb/f17/2023.1","DOIUrl":null,"url":null,"abstract":"Adhesion GPCRs are structurally identified on the basis of a large extracellular region, similar to the Class B GPCR, but which is linked to the 7TM region by a GPCR autoproteolysis-inducing (GAIN) domain [10] containing a GPCR proteolysis site (GPS). The N-terminal extracellular region often shares structural homology with adhesive domains (e.g. cadherins, immunolobulin, lectins) facilitating inter- and matricellular interactions and leading to the term adhesion GPCR [104, 418]. Several receptors have been suggested to function as mechanosensors [320, 288, 396, 38]. Cryo-EM structures of the 7-transmembrane domain of several adhesion GPCRs have been determined recently [292, 21, 403, 212, 300, 302, 431, 293]. The nomenclature of these receptors was revised in 2015 as recommended by NC-IUPHAR and the Adhesion GPCR Consortium [125].","PeriodicalId":14617,"journal":{"name":"IUPHAR/BPS Guide to Pharmacology CITE","volume":"74 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2023-04-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Adhesion Class GPCRs in GtoPdb v.2023.1\",\"authors\":\"Demet Arac-Ozkan, Gabriela Aust, Tom I. Bonner, Heike Cappallo-Obermann, Caroline Formstone, Jörg Hamann, Breanne Harty, Henrike Heyne, Christiane Kirchhoff, Barbara Knapp, Arunkumar Krishnan, Tobias Langenhan, Diana Le Duc, Hsi-Hsien Lin, David C. Martinelli, Kelly Monk, Xianhua Piao, Simone Prömel, Torsten Schöneberg, Helgi Schiöth, Kathleen Singer, Martin Stacey, Yuri Ushkaryov, Uwe Wolfrum, Lei Xu\",\"doi\":\"10.2218/gtopdb/f17/2023.1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Adhesion GPCRs are structurally identified on the basis of a large extracellular region, similar to the Class B GPCR, but which is linked to the 7TM region by a GPCR autoproteolysis-inducing (GAIN) domain [10] containing a GPCR proteolysis site (GPS). The N-terminal extracellular region often shares structural homology with adhesive domains (e.g. cadherins, immunolobulin, lectins) facilitating inter- and matricellular interactions and leading to the term adhesion GPCR [104, 418]. Several receptors have been suggested to function as mechanosensors [320, 288, 396, 38]. Cryo-EM structures of the 7-transmembrane domain of several adhesion GPCRs have been determined recently [292, 21, 403, 212, 300, 302, 431, 293]. The nomenclature of these receptors was revised in 2015 as recommended by NC-IUPHAR and the Adhesion GPCR Consortium [125].\",\"PeriodicalId\":14617,\"journal\":{\"name\":\"IUPHAR/BPS Guide to Pharmacology CITE\",\"volume\":\"74 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2023-04-26\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"IUPHAR/BPS Guide to Pharmacology CITE\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2218/gtopdb/f17/2023.1\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"IUPHAR/BPS Guide to Pharmacology CITE","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2218/gtopdb/f17/2023.1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Adhesion GPCRs are structurally identified on the basis of a large extracellular region, similar to the Class B GPCR, but which is linked to the 7TM region by a GPCR autoproteolysis-inducing (GAIN) domain [10] containing a GPCR proteolysis site (GPS). The N-terminal extracellular region often shares structural homology with adhesive domains (e.g. cadherins, immunolobulin, lectins) facilitating inter- and matricellular interactions and leading to the term adhesion GPCR [104, 418]. Several receptors have been suggested to function as mechanosensors [320, 288, 396, 38]. Cryo-EM structures of the 7-transmembrane domain of several adhesion GPCRs have been determined recently [292, 21, 403, 212, 300, 302, 431, 293]. The nomenclature of these receptors was revised in 2015 as recommended by NC-IUPHAR and the Adhesion GPCR Consortium [125].
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