1ZLC
Solution Conformation of alpha-conotoxin PIA
Summary for 1ZLC
| Entry DOI | 10.2210/pdb1zlc/pdb |
| NMR Information | BMRB: 6720 |
| Descriptor | Alpha-conotoxin PIA (1 entity in total) |
| Functional Keywords | alpha-helix, beta-turn, two disulfide bonds, c-terminal amidation, toxin |
| Cellular location | Secreted (By similarity): P69658 |
| Total number of polymer chains | 1 |
| Total formula weight | 1986.30 |
| Authors | Chi, S.-W.,Lee, S.-H.,Kim, D.-H.,Kim, J.-S.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (deposition date: 2005-05-05, release date: 2006-05-02, Last modification date: 2024-10-23) |
| Primary citation | Chi, S.-W.,Lee, S.-H.,Kim, D.-H.,Kim, J.-S.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. Solution structure of alpha-conotoxin PIA, a novel antagonist of alpha6 subunit containing nicotinic acetylcholine receptors Biochem.Biophys.Res.Commun., 338:1990-1997, 2005 Cited by PubMed Abstract: alpha-Conotoxin PIA is a novel nicotinic acetylcholine receptor (nAChR) antagonist isolated from Conus purpurascens that targets nAChR subtypes containing alpha6 and alpha3 subunits. alpha-conotoxin PIA displays 75-fold higher affinity for rat alpha6/alpha3beta2beta3 nAChRs than for rat alpha3beta2 nAChRs. We have determined the three-dimensional structure of alpha-conotoxin PIA by nuclear magnetic resonance spectroscopy. The alpha-conotoxin PIA has an "omega-shaped" overall topology as other alpha4/7 subfamily conotoxins. Yet, unlike other neuronally targeted alpha4/7-conotoxins, its N-terminal tail Arg1-Asp2-Pro3 protrudes out of its main molecular body because Asp2-Pro3-Cys4-Cys5 forms a stable type I beta-turn. In addition, a kink introduced by Pro15 in the second loop of this toxin provides a distinct steric and electrostatic environment from those in alpha-conotoxins MII and GIC. By comparing the structure of alpha-conotoxin PIA with other functionally related alpha-conotoxins we suggest structural features in alpha-conotoxin PIA that may be associated with its unique receptor recognition profile. PubMed: 16289101DOI: 10.1016/j.bbrc.2005.10.176 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
