Initial crystallographic studies of visual arrestin: Insights and perspectives

Joel A. Hirsch*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Crystallographic studies of visual arrestin in the late nineties built upon fundamental biochemical work that had identified arrestins as proteins central to desensitization of GPCR signaling. The structural findings revealed the arrestin fold that had two related domains and a C-tail, which folded onto the molecule's surface. The structures had a curious "polar core" that sat at the fulcrum of the two domains and which acts as an active site for conformational activation. The structures also served as the basis for elaborating the arrestin fold, found in all the kingdoms of life. Finally, the results suggested that quaternary structure i.e. The oligomeric state played a role in self-regulation.

Original languageEnglish
Title of host publicationThe Structural Basis of Arrestin Functions
PublisherSpringer International Publishing
Pages33-42
Number of pages10
ISBN (Electronic)9783319575537
ISBN (Print)9783319575520
DOIs
StatePublished - 24 May 2017

Keywords

  • Activation
  • Arrestin
  • Arrestin fold
  • Conformational change
  • Crystal structure
  • Phosphate sensor

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