1K2A
Modified Form of Eosinophil-derived Neurotoxin
1K2A の概要
| エントリーDOI | 10.2210/pdb1k2a/pdb |
| 分子名称 | eosinophil-derived neurotoxin, SULFATE ION (3 entities in total) |
| 機能のキーワード | rnase a folding, hydrolase |
| 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 | 15909.96 |
| 構造登録者 | Chang, C.,Newton, D.L.,Rybak, S.M.,Wlodawer, A. (登録日: 2001-09-26, 公開日: 2002-04-03, 最終更新日: 2024-11-06) |
| 主引用文献 | Chang, C.,Newton, D.L.,Rybak, S.M.,Wlodawer, A. Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities. J.Mol.Biol., 317:119-130, 2002 Cited by PubMed Abstract: The crystal structure of a post-translationally modified form of eosinophil-derived neurotoxin (EDN) with four extra residues on its N terminus ((-4)EDN) has been solved and refined at atomic resolution (1 A). Two of the extra residues can be placed unambiguously, while the density corresponding to two others is poor. The modified N terminus appears to influence the position of the catalytically important His129, possibly explaining the diminished catalytic activity of this variant. However, (-4)EDN has been shown to be cytotoxic to a Kaposi's sarcoma tumor cell line and other endothelial cell lines. Analysis of the structure and function suggests that the reason for cytotoxicity is most likely due to cellular recognition by the N-terminal extension, since the intrinsic activity of the enzyme is not sufficient for cytotoxicity and the N-terminal extension does not affect the conformation of EDN. PubMed: 11916383DOI: 10.1006/jmbi.2002.5406 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1 Å) |
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