5IPO
Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
Summary for 5IPO
| Entry DOI | 10.2210/pdb5ipo/pdb |
| NMR Information | BMRB: 30033 |
| Descriptor | Hge-scorpine (1 entity in total) |
| Functional Keywords | scorpine-like peptide, hadrurus gertschi, antiparasitic activity, toxin |
| Biological source | Hadrurus gertschi (Scorpion) |
| Cellular location | Secreted: Q0GY40 |
| Total number of polymer chains | 1 |
| Total formula weight | 5310.27 |
| Authors | Flores-Solis, D.,Rodriguez De La Vega, R.,del Rio-Portilla, F. (deposition date: 2016-03-09, release date: 2016-06-29, Last modification date: 2024-11-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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