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":"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}
引用次数: 0
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].