1JSY

Crystal structure of bovine arrestin-2

Summary for 1JSY

• Entry DOI: 10.2210/pdb1jsy/pdb
• Descriptor: Bovine arrestin-2 (full length) (2 entities in total)
• Functional Keywords: nonvisual arrestins, beta-arrestins, desensitization, endocytosis, down-regulation, signaling protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P17870
• Total number of polymer chains: 1
• Total formula weight: 47201.69

Authors

Milano, S.K.,Pace, H.C.,Kim, Y.M.,Brenner, C.,Benovic, J.L. (deposition date: 2001-08-19, release date: 2002-03-27, Last modification date: 2023-08-16)

Primary citation

Milano, S.K.,Pace, H.C.,Kim, Y.M.,Brenner, C.,Benovic, J.L.
Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.
Biochemistry, 41:3321-3328, 2002

PubMed 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.

PubMed: 11876640
DOI: 10.1021/bi015905j

Experimental method

X-RAY DIFFRACTION (2.9 Å)