7QNV

human carbonic anhydrase II bound to 3-methylbenzoselenoate

これはPDB形式変換不可エントリーです。

7QNV の概要

• エントリーDOI: 10.2210/pdb7qnv/pdb
• 分子名称: Carbonic anhydrase 2, ZINC ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: carbonic anhydrase 2, inhibitor, metalloenzyme, selenoate, lyase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29844.78

構造登録者

Angeli, A.,Ferraroni, M. (登録日: 2021-12-22, 公開日: 2023-01-18, 最終更新日: 2024-01-31)

主引用文献

Tanini, D.,Capperucci, A.,Locuoco, M.,Ferraroni, M.,Costantino, G.,Angeli, A.,Supuran, C.T.
Benzoselenoates: A novel class of carbonic anhydrase inhibitors.
Bioorg.Chem., 122:105751-105751, 2022

PubMed Abstract: A series of benzoselenoates has been prepared and their inhibitory properties against the most relevant human Carbonic Anhydrases (CAs) isoforms, among which hCA I, II, IV, VII, IX, and XII were investigated. These inhibitors were designed considering the carboxylates and mono-/dithiocarbamates as lead and led to the observation that the COSe is a new zinc-binding group (ZBG) for metalloenzymes possessing zinc ions at their active site. The substitution pattern on aromatic ring of the benzoselenoates is the crucial structural element influencing selectivity towards various isoforms. We elucidated the binding mode of benzoselenoates to hCA I and hCA II by using X-ray crystallography. The negatively charged selenium atom from the new ZBG was observed coordinated to the zinc ion from the CA active site at a distance of 2.30-2.40 Å from it. Overall, these data might be useful for the development of new inhibitors with higher selectivity and efficacy for various hCAs.

PubMed: 35344894
DOI: 10.1016/j.bioorg.2022.105751

実験手法

X-RAY DIFFRACTION (1.278 Å)