› 2jus

Solution NMR

alpha RgIA, a Novel Conotoxin that Blocks the alpha9-alpha10 nAChR

Released:
DOI: 10.2210/pdb2jus/pdb
PDB entry 2jus coloured by chain, ensemble of 20 models, front view.
PDB entry 2jus coloured by chain, ensemble of 20 models, side view.
PDB entry 2jus coloured by chain, ensemble of 20 models, top view.
Source organism: Conus regius
Primary publication:
Alpha-RgIA, a novel conotoxin that blocks the alpha9alpha10 nAChR: structure and identification of key receptor-binding residues.
Ellison M, Feng ZP, Park AJ, Zhang X, Olivera BM, McIntosh JM, Norton RS
J Mol Biol 377 1216-27 (2008)
PMID: 18295795

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142952 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-conotoxin RgIA Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.6 KDa
Source organism: Conus regius
Expression system: Not provided
UniProt:
  • Canonical: P0C1D0 (Residues: 20-32; Coverage: 41%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

22 review citations

Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system.
Taly et al. (2009)
21 more

3 mentions without citation

Alpha-RgIA, a novel conotoxin that blocks the alpha9alpha10 nAChR: structure and identification of key receptor-binding residues.
Ellison et al. (2008)
2 more