5IPO
Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
5IPO の概要
| エントリーDOI | 10.2210/pdb5ipo/pdb |
| NMR情報 | BMRB: 30033 |
| 分子名称 | Hge-scorpine (1 entity in total) |
| 機能のキーワード | scorpine-like peptide, hadrurus gertschi, antiparasitic activity, toxin |
| 由来する生物種 | Hadrurus gertschi (Scorpion) |
| 細胞内の位置 | Secreted: Q0GY40 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 5310.27 |
| 構造登録者 | Flores-Solis, D.,Rodriguez De La Vega, R.,del Rio-Portilla, F. (登録日: 2016-03-09, 公開日: 2016-06-29, 最終更新日: 2024-11-20) |
| 主引用文献 | Flores-Solis, D.,Toledano, Y.,Rodriguez-Lima, O.,Cano-Sanchez, P.,Ramirez-Cordero, B.E.,Landa, A.,Rodriguez de la Vega, R.C.,Del Rio-Portilla, F. Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi. Febs Lett., 590:2286-2296, 2016 Cited by PubMed Abstract: Scorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channel-blocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold. PubMed: 27314815DOI: 10.1002/1873-3468.12255 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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