ISDA: 1J5J

Deposition Date 2002-04-16

Release Date 2002-11-20

Last Version Date 2024-10-16

Entry Detail

PDB ID:

1J5J

Keywords:

TOXIN

Title:

Solution structure of HERG-specific scorpion toxin BeKm-1

Biological Source:

Source Organism(s):

Mesobuthus eupeus (Taxon ID: 34648)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

SOLUTION NMR

Conformers Submitted:

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:BeKm-1 toxin
Chain IDs:A
Chain Length:36
Number of Molecules:1
Biological Source:Mesobuthus eupeus

UniProt ID:Q9BKB7 Pfam ID:PF00451

Ligand Molecules

Primary Citation

New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1.

Korolkova, Y.V, Bocharov, E.V, Angelo, K, Maslennikov, I.V, Grinenko, O.V, Lipkin, A.V, Nosyreva, E.D, Pluzhnikov, K.A, Olesen, S.P, Arseniev, A.S, Grishin, E.V, Korolkova, Y.V, Kozlov, S.A, Lipkin, A.V, Pluzhnikov, K.A, Hadley, J.K, Filippov, A.K, Brown, D.A, Angelo, K, Strobek, D, Jespersen, T, Olesen, S.P, Jensen, B.S, Grishin, E.V.Show

J.Biol.Chem. 277 43104 43109 (2002)

PMID: 12151390 DOI: 10.1074/jbc.M204083200

Abstact

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.

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Primary Citation of related structures

Abstact

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