1GQV

Atomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin

1GQV の概要

• エントリーDOI: 10.2210/pdb1gqv/pdb
• 関連するPDBエントリー: 1HI2 1HI3 1HI4 1HI5
• 分子名称: EOSINOPHIL-DERIVED NEUROTOXIN, ACETATE ION (3 entities in total)
• 機能のキーワード: rnase-2, rnase us, ribonuclease
• 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: 15670.79

構造登録者

Swaminathan, G.J.,Holloway, D.E.,Veluraja, K.,Acharya, K.R. (登録日: 2001-12-05, 公開日: 2002-03-08, 最終更新日: 2024-10-23)

主引用文献

Swaminathan, G.J.,Holloway, D.E.,Veluraja, K.,Acharya, K.R.
Atomic Resolution (0.98 A) Structure of Eosinophil-Derived Neurotoxin
Biochemistry, 41:3341-, 2002

PubMed Abstract: Human eosinophil-derived neurotoxin (EDN) is a small, basic protein that belongs to the ribonuclease A superfamily. EDN displays antiviral activity and causes the neurotoxic Gordon phenomenon when injected into rabbits. Although EDN and ribonuclease A have appreciable structural similarity and a conserved catalytic triad, their peripheral substrate-binding sites are not conserved. The crystal structure of recombinant EDN (rEDN) has been determined at 0.98 A resolution from data collected at a low temperature (100 K). We have refined the crystallographic model of the structure using anisotropic displacement parameters to a conventional R-factor of 0.116. This represents the highest resolution structure of rEDN determined to date and is only the second ribonuclease structure to be determined at a resolution greater than 1.0 A. The structure provides a detailed picture of the conformational freedom at the various subsites of rEDN, and the water structure accounts for more than 50% of the total solvent content of the unit cell. This information will be crucial for the design of tight-binding inhibitors to restrain the ribonucleolytic activity of rEDN.

PubMed: 11876642
DOI: 10.1021/BI015911F

実験手法

X-RAY DIFFRACTION (0.98 Å)