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Biochemistry. 2002 Mar 12;41(10):3321-8.

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.

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Structural Biology and Bioinformatics Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.


Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction.

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