2GEH

N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors

2GEH の概要

• エントリーDOI: 10.2210/pdb2geh/pdb
• 分子名称: Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (5 entities in total)
• 機能のキーワード: carbonic anhydrase, inhibitors, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P00918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29831.71

構造登録者

Temperini, C.,Innocenti, A.,Scozzafava, A.,Supuran, C.T. (登録日: 2006-03-20, 公開日: 2006-06-20, 最終更新日: 2024-02-14)

主引用文献

Temperini, C.,Innocenti, A.,Scozzafava, A.,Supuran, C.T.
N-Hydroxyurea-A versatile zinc binding function in the design of metalloenzyme inhibitors.
Bioorg.Med.Chem.Lett., 16:4316-4320, 2006

PubMed Abstract: N-Hydroxyurea binds both to carbonic anhydrase (CA) and to matrix metalloproteinases (MMPs). X-ray crystallography showed N-hydroxyurea to bind in a bidentate mode by means of the oxygen and nitrogen atoms of the NHOH moiety to the Zn(II) ion of CA, participating in a network of hydrogen bonds with a water molecule and Thr199. A derivatized N-hydroxyurea showed low-micromolar affinity for several CAs. This simple zinc binding function may be exploited for obtaining potent metalloenzyme inhibitors, due to its versatility of binding to the metal ion present in the active site of such enzymes.

PubMed: 16759856
DOI: 10.1016/j.bmcl.2006.05.068

実験手法

X-RAY DIFFRACTION (2 Å)