7M1E
Structural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domains
Summary for 7M1E
| Entry DOI | 10.2210/pdb7m1e/pdb |
| NMR Information | BMRB: 30879 |
| Descriptor | Scorpine (1 entity in total) |
| Functional Keywords | scorpion toxins, potassium channels, scorpine like-peptides, cytolytic peptides, toxin |
| Biological source | Pandinus imperator (Emperor scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 3135.68 |
| Authors | del Rio, J.F.,Lopez, A.E.,Titaux, G. (deposition date: 2021-03-12, release date: 2022-01-19, Last modification date: 2024-05-15) |
| Primary citation | Lopez-Giraldo, E.,Carrillo, E.,Titaux-Delgado, G.,Cano-Sanchez, P.,Colorado, A.,Possani, L.D.,Rio-Portilla, F.D. Structural and functional studies of scorpine: A channel blocker and cytolytic peptide. Toxicon, 222:106985-106985, 2022 Cited by PubMed Abstract: Scorpine is an antimicrobial and antimalarial peptide isolated from Pandinus imperator scorpion venom. As there are few functional and structural studies reported on scorpine-like peptides, we investigated the recombinant truncated N- and C-terminal domains as well as complete scorpine using biological assays and determined the N- and C-terminal structures using solution nuclear magnetic resonance. The study was conducted using recombinant N- and C-terminal peptides and complete scorpine expressed in Escherichia coli. The results showed that N-scorpine presented a random coil structure in water and adopted α-helical folding in the presence of 50% trifluoroethanol (TFE). C-scorpine contains three disulfide bonds with two structural domains: an unstructured N-terminal domain in water that can form a typical secondary alpha-helix structure in 50% TFE and a C-terminal domain with the CS-αβ motif. Our findings demonstrate cytolytic activity associated with C-scorpine, N-scorpine, and scorpine, as well as channel blocking activity associated with the C-scorpine domain. PubMed: 36436588DOI: 10.1016/j.toxicon.2022.106985 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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