2GCZ
Solution Structure of alpha-Conotoxin OmIA
Summary for 2GCZ
| Entry DOI | 10.2210/pdb2gcz/pdb |
| Descriptor | Alpha-conotoxin OmIA (1 entity in total) |
| Functional Keywords | alpha-helix, beta-turn, two disulfide bonds, c-terminal amidation, toxin |
| Biological source | Conus omaria (Omaria cone) |
| Total number of polymer chains | 1 |
| Total formula weight | 1725.97 |
| Authors | Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (deposition date: 2006-03-15, release date: 2006-07-25, Last modification date: 2024-11-20) |
| Primary citation | Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes Biochem.Biophys.Res.Commun., 345:248-254, 2006 Cited by PubMed Abstract: alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that shows a approximately 20-fold higher affinity to the alpha3beta2 over the alpha6beta2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of alpha-conotoxin OmIA by nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an "omega-shaped" overall topology with His(5)-Asn(12) forming an alpha-helix. Structural features of alpha-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related alpha4/7 subfamily conotoxins. Reduced size of the hydrophilic area in alpha-conotoxin OmIA seems to be associated with the reduced affinity towards the alpha6beta2 nAChR subtype. PubMed: 16678128DOI: 10.1016/j.bbrc.2006.04.099 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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