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Solution NMR

SOLUTION STRUCTURE OF PO5-NH2, A SCORPION TOXIN ANALOG WITH HIGH AFFINITY FOR THE APAMIN-SENSITIVE POTASSIUM CHANNEL

Released:
DOI: 10.2210/pdb1pnh/pdb
PDB entry 1pnh coloured by chain, ensemble of 25 models, front view.
PDB entry 1pnh coloured by chain, ensemble of 25 models, side view.
PDB entry 1pnh coloured by chain, ensemble of 25 models, top view.
Source organism: Androctonus mauritanicus mauritanicus
Primary publication:
Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel.
Meunier S, Bernassau JM, Sabatier JM, Martin-Eauclaire MF, Van Rietschoten J, Cambillau C, Darbon H
Biochemistry 32 11969-76 (1993)
PMID: 8218272

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152075 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 5.2 Chain: A
Molecule details ›
Chain: A
Length: 31 amino acids
Theoretical weight: 3.43 KDa
Source organism: Androctonus mauritanicus mauritanicus
Expression system: Not provided
UniProt:
  • Canonical: P31719 (Residues: 1-31; Coverage: 100%)
Sequence domains: Scorpion short toxin, BmKK2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

1 review citation

Synthetic peptides as tools to investigate the structure and pharmacology of potassium channel-acting short-chain scorpion toxins.
Lecomte et al. (1998)
32 other articles

3 mentions without citation

Sequence variations within protein families are linearly related to structural variations.
Koehl et al. (2002)
2 more