2PFG

Crystal structure of human CBR1 in complex with BiGF2.

2PFG の概要

• エントリーDOI: 10.2210/pdb2pfg/pdb
• 関連するPDBエントリー: 1WMA
• 分子名称: Carbonyl reductase [NADPH] 1, CHLORIDE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: glutathione, macro molecule, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P16152
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31517.08

構造登録者

Rauh, D.,Bateman, R.L.,Shokat, K.M. (登録日: 2007-04-04, 公開日: 2007-09-25, 最終更新日: 2023-11-15)

主引用文献

Bateman, R.,Rauh, D.,Shokat, K.M.
Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct.
Org.Biomol.Chem., 5:3363-3367, 2007

PubMed Abstract: Glutathione forms complex reaction products with formaldehyde, which can be further modified through enzymatic modification. We studied the non-enzymatic reaction between glutathione and formaldehyde and identified a bicyclic complex containing two equivalents of formaldehyde and one glutathione molecule by protein X-ray crystallography (PDB accession number 2PFG). We have also used (1)H, (13)C and 2D NMR spectroscopy to confirm the structure of this unusual adduct. The key feature of this adduct is the involvement of the gamma-glutamyl alpha-amine and the Cys thiol in the formation of the bicyclic ring structure. These findings suggest that the structure of GSH allows for bi-dentate masking of the reactivity of formaldehyde. As this species predominates at near physiological pH values, we suggest this adduct may have biological significance.

PubMed: 17912391
DOI: 10.1039/b707602a

実験手法

X-RAY DIFFRACTION (1.54 Å)