1HI2

Eosinophil-derived Neurotoxin (EDN) - Sulphate Complex

1HI2 の概要

• エントリーDOI: 10.2210/pdb1hi2/pdb
• 関連するPDBエントリー: 1HI3 1HI4 1HI5
• 分子名称: EOSINOPHIL-DERIVED NEUROTOXIN, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, rnase-2, rnase us, ribonuclease
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Lysosome (Probable): P10153
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15803.88

構造登録者

Leonidas, D.D.,Boix, E.,Prill, R.,Suzuki, M.,Turton, R.,Minson, K.,Swaminathan, G.J.,Youle, R.J.,Acharya, K.R. (登録日: 2001-01-02, 公開日: 2001-05-31, 最終更新日: 2024-11-20)

主引用文献

Leonidas, D.D.,Boix, E.,Prill, R.,Suzuki, M.,Turton, R.,Minson, K.,Swaminathan, G.J.,Youle, R.J.,Acharya, K.R.
Mapping the Ribonucleolytic Active Site of Eosinophil-Derived Neurotoxin (Edn): High Resolution Crystal Structures of Edn Complexes with Adenylic Nucleotide Inhibitors
J.Biol.Chem., 276:15009-, 2001

PubMed Abstract: Eosinophil-derived neurotoxin (EDN), a basic ribonuclease found in the large specific granules of eosinophils, belongs to the pancreatic RNase A family. Although its physiological function is still unclear, it has been shown that EDN is a neurotoxin capable of inducing the Gordon phenomenon in rabbits. EDN is also a potent helminthotoxin and can mediate antiviral activity of eosinophils against isolated virions of the respiratory syncytial virus. EDN is a catalytically efficient RNase sharing similar substrate specificity with pancreatic RNase A with its ribonucleolytic activity being absolutely essential for its neurotoxic, helminthotoxic, and antiviral activities. The crystal structure of recombinant human EDN in the unliganded form has been determined previously (Mosimann, S. C., Newton, D. L., Youle, R. J., and James, M. N. G. (1996) J. Mol. Biol. 260, 540-552). We have now determined high resolution (1.8 A) crystal structures for EDN in complex with adenosine-3',5'-diphosphate (3',5'-ADP), adenosine-2',5'-di-phosphate (2',5'-ADP), adenosine-5'-diphosphate (5'-ADP) as well as for a native structure in the presence of sulfate refined at 1.6 A. The inhibition constant of these mononucleotides for EDN has been determined. The structures present the first detailed picture of differences between EDN and RNase A in substrate recognition at the ribonucleolytic active site. They also provide a starting point for the design of tight-binding inhibitors, which may be used to restrain the RNase activity of EDN.

PubMed: 11154698
DOI: 10.1074/JBC.M010585200

実験手法

X-RAY DIFFRACTION (1.6 Å)