5EQO

Human Angiogenin in complex with sulphate anions at an acidic solution

5EQO の概要

• エントリーDOI: 10.2210/pdb5eqo/pdb
• 分子名称: Angiogenin, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle lumen : P03950
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14491.11

構造登録者

Chatzileontiadou, D.S.M.,Leonidas, D.D. (登録日: 2015-11-13, 公開日: 2016-08-17, 最終更新日: 2024-10-23)

主引用文献

Chatzileontiadou, D.S.,Tsirkone, V.G.,Dossi, K.,Kassouni, A.G.,Liggri, P.G.,Kantsadi, A.L.,Stravodimos, G.A.,Balatsos, N.A.,Skamnaki, V.T.,Leonidas, D.D.
The ammonium sulfate inhibition of human angiogenin.
Febs Lett., 590:3005-3018, 2016

PubMed Abstract: In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin (IC50 = 123.5 ± 14.9 mm) is comparable to that previously reported for RNase A (119.0 ± 6.5 mm) and RNase 2 (95.7 ± 9.3 mm). However, analysis of two X-ray crystal structures of human angiogenin in complex with sulfate anions (in acidic and basic pH environments, respectively) indicates an entirely distinct mechanism of inhibition. While ammonium sulfate inhibits the ribonucleolytic activity of RNase A and RNase 2 by binding to the active site of these enzymes, sulfate anions bind only to peripheral substrate anion-binding subsites of human angiogenin, and not to the active site.

PubMed: 27483019
DOI: 10.1002/1873-3468.12335

実験手法

X-RAY DIFFRACTION (2.4 Å)