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alpha-RgIA, a Novel Conotoxin that Blocks the nAChR
Authors
Feng, Z., Ellison, M., Park, A., Zhang, X., McIntosh, M., Olivera, B., Norton, R.
Assembly
toxin
Entity
1. toxin (polymer, Thiol state: all disulfide bound), 13 monomers, 1489.727 Da Detail

GCCSDPRCAY RCR


Formula weight
1489.727 Da
Source organism
Conus regius
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 98.6 %, Completeness (bb): 96.2 % Detail

Polymer type: polypeptide(L)

Total1H
All98.6 % (71 of 72)98.6 % (71 of 72)
Backbone96.2 % (25 of 26)96.2 % (25 of 26)
Sidechain100.0 % (46 of 46)100.0 % (46 of 46)
Aromatic100.0 % (4 of 4)100.0 % (4 of 4)
Methyl100.0 % (1 of 1)100.0 % (1 of 1)

1. RgIA

GCCSDPRCAY RCR

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5.1


#NameIsotope labelingTypeConcentration
1RgIAnatural abundance0.6 mM
2D2O[U-100% 2H]5 %
3H2O95 %

Release date
2008-03-12
Citation
Alpha-RgIA, a novel conotoxin that blocks the alpha9alpha10 nAChR: structure and identification of key receptor-binding residues
Ellison, M., Feng, Z., Park, A., Zhang, X., McIntosh, M., Olivera, B., Norton, R.
J. Mol. Biol. (2008), 377, 1216-1227, PubMed 18295795 , DOI 10.1016/j.jmb.2008.01.082 ,
Related entities 1. toxin, : 1 : 5 : 23 entities Detail
Interaction partners 1. toxin, : 1 interactors Detail
Experiments performed 3 experiments Detail
Chemical shift validation 3 contents Detail
Keywords conotoxin, nicotinic acetylcholine receptor, NMR, pain, peptide, structure