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Solution NMR

NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES

Released:
DOI: 10.2210/pdb1cmr/pdb
PDB entry 1cmr coloured by chain, ensemble of 18 models, front view.
PDB entry 1cmr coloured by chain, ensemble of 18 models, side view.
PDB entry 1cmr coloured by chain, ensemble of 18 models, top view.
Source organism: Leiurus hebraeus
Primary publication:
Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein.
Zinn-Justin S, Guenneugues M, Drakopoulou E, Gilquin B, Vita C, Ménez A
Biochemistry 35 8535-43 (1996)
PMID: 8679614

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146605 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium channel toxin alpha-KTx 1.1 Chain: A
Molecule details ›
Chain: A
Length: 31 amino acids
Theoretical weight: 3.57 KDa
Source organism: Leiurus hebraeus
Expression system: Not provided
UniProt:
  • Canonical: P13487 (Residues: 29-59; Coverage: 84%)
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

4 review citations

Chlorotoxin: Structure, activity, and potential uses in cancer therapy.
Ojeda et al. (2016)
3 more

4 mentions without citation

Peptide toxins and small-molecule blockers of BK channels.
Yu et al. (2016)
3 more