Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide

Arun K. Shukla, Aashish Manglik, Andrew C. Kruse, Kunhong Xiao, Rosana I. Reis, Wei-Chou Tseng, Dean P. Staus, Daniel Hilger, Serdar Uysal, Li-Yin Huang, Marcin Paduch, Prachi Tripathi-Shukla, Akiko Koide, Shohei Koide, William I. Weis, Anthony A. Kossiakoff, Brian K. Kobilka () and Robert J. Lefkowitz ()
Additional contact information
Arun K. Shukla: Duke University Medical Center
Aashish Manglik: Molecular and Cellular Physiology, Stanford University School of Medicine
Andrew C. Kruse: Molecular and Cellular Physiology, Stanford University School of Medicine
Kunhong Xiao: Duke University Medical Center
Rosana I. Reis: Duke University Medical Center
Wei-Chou Tseng: Duke University Medical Center
Dean P. Staus: Duke University Medical Center
Daniel Hilger: Molecular and Cellular Physiology, Stanford University School of Medicine
Serdar Uysal: University of Chicago
Li-Yin Huang: Duke University Medical Center
Marcin Paduch: University of Chicago
Prachi Tripathi-Shukla: Duke University Medical Center
Akiko Koide: University of Chicago
Shohei Koide: University of Chicago
William I. Weis: Molecular and Cellular Physiology, Stanford University School of Medicine
Anthony A. Kossiakoff: University of Chicago
Brian K. Kobilka: Molecular and Cellular Physiology, Stanford University School of Medicine
Robert J. Lefkowitz: Duke University Medical Center

Nature, 2013, vol. 497, issue 7447, 137-141

Abstract: The crystal structure of β-arrestin-1 in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the V2 vasopressin receptor is reported; the structure of the complex shows striking conformational differences in β-arrestin-1 when compared with its inactive conformation.

Date: 2013
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DOI: 10.1038/nature12120

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