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Solution NMR

SOLUTION STRUCTURE OF HPTX2, A TOXIN FROM HETEROPODA VENATORIA SPIDER VENOM THAT BLOCKS KV4.2 POTASSIUM CHANNEL

Released:
DOI: 10.2210/pdb1emx/pdb
PDB entry 1emx coloured by chain, ensemble of 26 models, front view.
PDB entry 1emx coloured by chain, ensemble of 26 models, side view.
PDB entry 1emx coloured by chain, ensemble of 26 models, top view.
Source organism: Heteropoda venatoria
Primary publication:
Solution structure of hpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel.
Bernard C, Legros C, Ferrat G, Bischoff U, Marquardt A, Pongs O, Darbon H
Protein Sci 9 2059-67 (2000)
PMID: 11152117

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kappa-sparatoxin-Hv1b Chain: A
Molecule details ›
Chain: A
Length: 30 amino acids
Theoretical weight: 3.42 KDa
Source organism: Heteropoda venatoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P58426 (Residues: 1-30; Coverage: 100%)
Sequence domains: Ion channel inhibitory toxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Transient outward potassium current, 'Ito', phenotypes in the mammalian left ventricle: underlying molecular, cellular and biophysical mechanisms.
Patel et al. (2005)
5 more

1 mention without citation

Effects of JZTX-V on the wild type Kv4.3 Expressed in HEK293T and Molecular Determinants in the Voltage-sensing Domains of Kv4.3 Interacting with JZTX-V.
Dehong et al. (2022)