Structural mechanism of arrestin activation

Curr Opin Struct Biol. 2017 Aug:45:160-169. doi: 10.1016/j.sbi.2017.05.001.

Patrick Scheerer ¹, Martha E Sommer ²

Affiliations

1 Institute of Medical Physics and Biophysics (CC2), Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany; Group Protein X-ray Crystallography & Signal Transduction, Germany. Electronic address: patrick.scheerer@charite.de.
2 Institute of Medical Physics and Biophysics (CC2), Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. Electronic address: martha.sommer@charite.de.

PMID: 28600951 DOI: 10.1016/j.sbi.2017.05.001

Abstract

The large and multifunctional family of G protein-coupled receptors (GPCRs) are regulated by a small family of structurally conserved Arrestin proteins. In order to bind an active GPCR, Arrestin must first be activated by interaction with the phosphorylated receptor C-terminus. Recent years have witnessed major developments in high-resolution crystal structures of pre-active arrestins and Arrestin or arrestin-derived Peptides in complex with an active GPCR. Although each structure individually offers only a limited snapshot, taken together and interpreted in light of recent complementary functional data, they offer valuable insight into how Arrestin is activated by and couples to a phosphorylated active GPCR.

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