1LGL: Solution structure of HERG-specific scorpion toxin BeKm-1

The scorpion toxin BeKm-1 is unique among a variety of known short scorpion toxins affecting potassium channels in its selective action on ether-a-go-go-related gene (ERG)-type channels. BeKm-1 shares the common molecular scaffold with other short scorpion toxins. The toxin spatial structure resolved by NMR consists of a short alpha-helix and a triple-stranded antiparallel beta-sheet. By toxin mutagenesis study we identified the residues that are important for the binding of BeKm-1 to the human ERG K+ (HERG) channel. The most critical residues (Tyr-11, Lys-18, Arg-20, Lys-23) are located in the alpha-helix and following loop whereas the "traditional" functional site of other short scorpion toxins is formed by residues from the beta-sheet. Thus the unique location of the binding site of BeKm-1 provides its specificity toward the HERG channel.
PDB ID: 1LGLDownload
MMDB ID: 21156
PDB Deposition Date: 2002/4/16
Updated in MMDB: 2002/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1LGL
Label Count Molecule
Protein (1 molecule)
Bekm-1 Toxin
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB