7WT0

human glyoxalase I (with C-ter His tag) in complex with TLSC702

7WT0 の概要

• エントリーDOI: 10.2210/pdb7wt0/pdb
• 分子名称: Lactoylglutathione lyase, ZINC ION, (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid, ... (4 entities in total)
• 機能のキーワード: glyoxalase i, zinc metalloenzyme, lyase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44531.32

構造登録者

Usami, M.,Yokoyama, H. (登録日: 2022-02-03, 公開日: 2022-04-13, 最終更新日: 2023-11-29)

主引用文献

Usami, M.,Ando, K.,Shibuya, A.,Takasawa, R.,Yokoyama, H.
Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.
Febs Lett., 596:1458-1467, 2022

PubMed Abstract: Human glyoxalase I (hGLO I) is an enzyme for detoxification of methylglyoxal (MG) and has been considered an attractive target for the development of new anticancer drugs. In our previous report, the GLO I inhibitor TLSC702 induced apoptosis in tumor cells. Here, we determined the crystal structures of hGLO I and its complex with TLSC702. In the complex, the carboxyl O atom of TLSC702 is coordinated to Zn , and TLSC702 mainly shows van der Waals interaction with hydrophobic residues. In the inhibitor-unbound structure, glycerol, which has similar functional groups to MG, was bound to Zn , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs.

PubMed: 35363883
DOI: 10.1002/1873-3468.14344

実験手法

X-RAY DIFFRACTION (2 Å)