Abstract：
: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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Milano SK,Pace HC,Kim YM,Brenner C,Benovic JLdoi
10.1021/bi015905jsubject
Has Abstractpub_date
2002-03-12 00:00:00pages
3321-8issue
10eissn
0006-2960issn
1520-4995pii
bi015905jjournal_volume
41pub_type
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