1JSY

Crystal structure of bovine arrestin-2

1JSY の概要

• エントリーDOI: 10.2210/pdb1jsy/pdb
• 分子名称: Bovine arrestin-2 (full length) (2 entities in total)
• 機能のキーワード: nonvisual arrestins, beta-arrestins, desensitization, endocytosis, down-regulation, signaling protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm: P17870
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47201.69

構造登録者

Milano, S.K.,Pace, H.C.,Kim, Y.M.,Brenner, C.,Benovic, J.L. (登録日: 2001-08-19, 公開日: 2002-03-27, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)