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

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.[1]

References

  1. Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Milano, S.K., Pace, H.C., Kim, Y.M., Brenner, C., Benovic, J.L. Biochemistry (2002) [Pubmed]
 
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