1NE5
Solution Structure of HERG Specific Scorpion Toxin CnErg1
Summary for 1NE5
| Entry DOI | 10.2210/pdb1ne5/pdb |
| NMR Information | BMRB: 5652 |
| Descriptor | ergtoxin (1 entity in total) |
| Functional Keywords | alpha-helix, triple-stranded beta-sheet, toxin |
| Cellular location | Secreted: Q86QT3 |
| Total number of polymer chains | 1 |
| Total formula weight | 4746.41 |
| Authors | Torres, A.M.,Paramjit, B.,Alewood, P.,Kuchel, P.W.,Vandenberg, J.I. (deposition date: 2002-12-10, release date: 2003-04-01, Last modification date: 2024-11-06) |
| Primary citation | Torres, A.M.,Bansal, P.,Alewood, P.F.,Bursill, J.A.,Kuchel, P.W.,Vandenberg, J.I. Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin FEBS Lett., 539:138-142, 2003 Cited by PubMed Abstract: The three-dimensional structure of chemically synthesized CnErg1 (Ergtoxin), which specifically blocks HERG (human ether-a-go-go-related gene) K+ channels, was determined by nuclear magnetic resonance spectroscopy. CnErg1 consists of a triple-stranded beta-sheet and an alpha-helix, as is typical of K+ channel scorpion toxins. The peptide structure differs from the canonical structures in that the first beta-strand is shorter and is nearer to the second beta-strand rather than to the third beta-strand on the C-terminus. There is also a large hydrophobic patch on the surface of the toxin, surrounding a central lysine residue, Lys13. We postulate that this hydrophobic patch is likely to form part of the binding surface of the toxin. PubMed: 12650941DOI: 10.1016/S0014-5793(03)00216-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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