5EQO

Human Angiogenin in complex with sulphate anions at an acidic solution

Summary for 5EQO

• Entry DOI: 10.2210/pdb5eqo/pdb
• Descriptor: Angiogenin, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasmic vesicle, secretory vesicle lumen : P03950
• Total number of polymer chains: 1
• Total formula weight: 14491.11

Authors

Chatzileontiadou, D.S.M.,Leonidas, D.D. (deposition date: 2015-11-13, release date: 2016-08-17, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)