Adhesion Class GPCRs in GtoPdb v.2023.1

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
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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].
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GtoPdb v.2023.1中粘附级gpcr
粘附GPCR在结构上基于一个大的细胞外区域进行识别,类似于B类GPCR,但它通过包含GPCR蛋白水解位点(GPS)的GPCR自蛋白水解诱导(GAIN)结构域[10]连接到7TM区域。n端细胞外区域通常与粘附结构域(如钙粘蛋白、免疫球蛋白、凝集素)具有结构同源性,促进细胞间和细胞基质相互作用,并导致术语粘附GPCR[104,418]。一些受体被认为具有机械传感器的功能[320,288,396,38]。最近研究人员已经确定了几种粘附gpcr的7-跨膜结构域的低温电镜结构[292,21,403,212,300,302,431,293]。根据NC-IUPHAR和粘附GPCR联盟的建议,这些受体的命名法在2015年进行了修订[125]。
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