The Arrestin-Receptor Complex: Exciting Answers and New Questions

  • Yanyong Kang
  • Karsten Melcher
  • Vsevolod V. GurevichEmail author
  • H. Eric XuEmail author


To better understand the molecular mechanism of arrestin-mediated signaling, detailed structural information on the arrestin-receptor complex is necessary. Biochemical studies provided some information about how arrestins are recruited by active receptors. The X-ray laser crystal structure of the rhodopsin–arrestin complex reveals unique structural features, which include the asymmetric binding of arrestin to rhodopsin. Arrestin adopts the active conformation, with a ~20° rotation between the N- and C-domains of the molecule, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. Rhodopsin–arrestin complex gives important insights into how G protein–coupled receptor signaling is terminated by arrestin and reveals structural basis of the mechanism of arrestin-biased signaling.


Crystal structure GPCR Rhodopsin Arrestin Biased signaling 


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Copyright information

© Springer International Publishing AG 2017

Authors and Affiliations

  1. 1.Laboratory of Structural Sciences, Center for Structural Biology and Drug DiscoveryVan Andel Research InstituteGrand RapidsUSA
  2. 2.Department of PharmacologyVanderbilt UniversityNashvilleUSA

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