2LI3
Structural and functional analysis of a novel potassium toxin argentinean scorpion Tityus trivittatus reveals a new kappa sub-family
Summary for 2LI3
| Entry DOI | 10.2210/pdb2li3/pdb |
| Descriptor | Potassium channel toxin kappa-KTX3.1 (1 entity in total) |
| Functional Keywords | alpha/alpha motif, alpha scorpion toxin, voltage gated potassium channel alpha toxin, toxin |
| Biological source | Tityus trivittatus (Argentinean scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 3334.92 |
| Authors | Saucedo-Yanez, A.,Del Rio-Portilla, F.,Hernandez-Lopez, R. (deposition date: 2011-08-19, release date: 2012-01-11, Last modification date: 2024-11-27) |
| Primary citation | Saucedo, A.L.,Flores-Solis, D.,Rodriguez de la Vega, R.C.,Ramirez-Cordero, B.,Hernandez-Lopez, R.,Cano-Sanchez, P.,Navarro, R.N.,Garcia-Valdes, J.,Coronas-Valderrama, F.,de Roodt, A.,Brieba, L.G.,Possani, L.D.,Del Rio-Portilla, F. New Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACING. J.Biol.Chem., 287:12321-12330, 2012 Cited by PubMed Abstract: Scorpion venoms are a rich source of K(+) channel-blocking peptides. For the most part, they are structurally related small disulfide-rich proteins containing a conserved pattern of six cysteines that is assumed to dictate their common three-dimensional folding. In the conventional pattern, two disulfide bridges connect an α-helical segment to the C-terminal strand of a double- or triple-stranded β-sheet, conforming a cystine-stabilized α/β scaffold (CSα/β). Here we show that two K(+) channel-blocking peptides from Tityus scorpions conserve the cysteine spacing of common scorpion venom peptides but display an unconventional disulfide pattern, accompanied by a complete rearrangement of the secondary structure topology into a CS helix-loop-helix fold. Sequence and structural comparisons of the peptides adopting this novel fold suggest that it would be a new elaboration of the widespread CSα/β scaffold, thus revealing an unexpected structural versatility of these small disulfide-rich proteins. Acknowledgment of such versatility is important to understand how venom structural complexity emerged on a limited number of molecular scaffolds. PubMed: 22238341DOI: 10.1074/jbc.M111.329607 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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