1QMW
Solution structure of alpha-conotoxin SI
Summary for 1QMW
| Entry DOI | 10.2210/pdb1qmw/pdb |
| NMR Information | BMRB: 4503 |
| Descriptor | ALPHA-CONOTOXIN SI (1 entity in total) |
| Functional Keywords | conotoxin, nicotinic acetylcholine receptor, toxin, venom |
| Biological source | CONUS STRIATUS (STRIATED CONE) |
| Total number of polymer chains | 1 |
| Total formula weight | 1357.64 |
| Authors | Benie, A.J.,Whitford, D.,Hargittai, B.,Barany, G.,Janes, R.W. (deposition date: 1999-10-08, release date: 2000-08-25, Last modification date: 2024-11-06) |
| Primary citation | Benie, A.J.,Whitford, D.,Hargittai, B.,Barany, G.,Janes, R.W. Solution Structure of Alpha-Conotoxin Si FEBS Lett., 476:287-, 2000 Cited by PubMed Abstract: The nuclear magnetic resonance solution structure of alpha-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that alpha-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of alpha-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue. PubMed: 10913630DOI: 10.1016/S0014-5793(00)01724-5 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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