1T1V

Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution

1T1V の概要

• エントリーDOI: 10.2210/pdb1t1v/pdb
• 分子名称: SH3 domain-binding glutamic acid-rich protein-like 3, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: glutaredoxin; thioredoxin fold; protein 3d-structure; x-ray crystallography, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm (By similarity): Q91VW3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21319.72

構造登録者

Nardini, M.,Mazzocco, M.,Massaro, M.,Maffei, M.,Vergano, A.,Donadini, A.,Scartezzini, M.,Bolognesi, M. (登録日: 2004-04-19, 公開日: 2004-06-29, 最終更新日: 2023-08-23)

主引用文献

Nardini, M.,Mazzocco, M.,Massaro, M.,Maffei, M.,Vergano, A.,Donadini, A.,Scartezzini, M.,Bolognesi, M.
Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 A resolution
Biochem.Biophys.Res.Commun., 318:470-476, 2004

PubMed Abstract: We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.

PubMed: 15120624
DOI: 10.1016/j.bbrc.2004.04.050

実験手法

X-RAY DIFFRACTION (1.6 Å)