› 1lup

Solution NMR

Solution structure of a toxin (GsMTx2) from the tarantula, Grammostola spatulata, which inhibits mechanosensitive ion channels

Released:
DOI: 10.2210/pdb1lup/pdb
PDB entry 1lup coloured by chain, ensemble of 20 models, front view.
PDB entry 1lup coloured by chain, ensemble of 20 models, side view.
PDB entry 1lup coloured by chain, ensemble of 20 models, top view.
Source organism: Grammostola rosea
Primary publication:
Solution structure of peptide toxins that block mechanosensitive ion channels.
Oswald RE, Suchyna TM, McFeeters R, Gottlieb P, Sachs F
J Biol Chem 277 34443-50 (2002)
PMID: 12082099

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kappa-theraphotoxin-Gr2a Chain: A
Molecule details ›
Chain: A
Length: 31 amino acids
Theoretical weight: 3.93 KDa
Source organism: Grammostola rosea
UniProt:
  • Canonical: P60273 (Residues: 1-31; Coverage: 100%)
Sequence domains: Ion channel inhibitory toxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing

Quick links

Citations

19 review citations

Therapeutic potential of venom peptides.
Lewis et al. (2003)
18 more

1 mention without citation

Molecular mechanism of the spider toxin κ-LhTx-I acting on the bacterial voltage-gated sodium channel NaChBac.
Xiao et al. (2022)