2A1A

PKR kinase domain-eIF2alpha Complex

2A1A の概要

• エントリーDOI: 10.2210/pdb2a1a/pdb
• 関連するPDBエントリー: 2A19
• 分子名称: Eukaryotic translation initiation factor 2 alpha subunit, Interferon-induced, double-stranded RNA-activated protein kinase (3 entities in total)
• 機能のキーワード: transferase, kinase, protein biosynthesis, protein synthesis-transferase complex, protein synthesis/transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53353.33

構造登録者

Dar, A.C.,Dever, T.E.,Sicheri, F. (登録日: 2005-06-19, 公開日: 2005-09-27, 最終更新日: 2023-08-23)

主引用文献

Dar, A.C.,Dever, T.E.,Sicheri, F.
Higher-Order Substrate Recognition of eIF2alpha by the RNA-Dependent Protein Kinase PKR.
Cell(Cambridge,Mass.), 122:887-900, 2005

PubMed Abstract: In response to binding viral double-stranded RNA byproducts within a cell, the RNA-dependent protein kinase PKR phosphorylates the alpha subunit of the translation initiation factor eIF2 on a regulatory site, Ser51. This triggers the general shutdown of protein synthesis and inhibition of viral propagation. To understand the basis for substrate recognition by and the regulation of PKR, we determined X-ray crystal structures of the catalytic domain of PKR in complex with eIF2alpha. The structures reveal that eIF2alpha binds to the C-terminal catalytic lobe while catalytic-domain dimerization is mediated by the N-terminal lobe. In addition to inducing a local unfolding of the Ser51 acceptor site in eIF2alpha, its mode of binding to PKR affords the Ser51 site full access to the catalytic cleft of PKR. The generality and implications of the structural mechanisms uncovered for PKR to the larger family of four human eIF2alpha protein kinases are discussed.

PubMed: 16179258
DOI: 10.1016/j.cell.2005.06.044

実験手法

X-RAY DIFFRACTION (2.8 Å)