1MXP
Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB
Summary for 1MXP
| Entry DOI | 10.2210/pdb1mxp/pdb |
| Related | 1MXN |
| Descriptor | alpha-conotoxin AuIB (1 entity in total) |
| Functional Keywords | turns, toxin |
| Cellular location | Secreted: P56640 |
| Total number of polymer chains | 1 |
| Total formula weight | 1575.79 |
| Authors | Dutton, J.L.,Bansal, P.S.,Hogg, R.C.,Adams, D.J.,Alewood, P.F.,Craik, D.J. (deposition date: 2002-10-03, release date: 2002-12-30, Last modification date: 2024-11-20) |
| Primary citation | Dutton, J.L.,Bansal, P.S.,Hogg, R.C.,Adams, D.J.,Alewood, P.F.,Craik, D.J. A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in alpha -Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity. J.Biol.Chem., 277:48849-48857, 2002 Cited by PubMed Abstract: alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer. PubMed: 12376538DOI: 10.1074/jbc.M208842200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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