1j5j

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5j OCA], [http://www.ebi.ac.uk/pdbsum/1j5j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j5j RCSB]</span>
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[[Category: cysteine-knot motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:29:07 2008''

Revision as of 18:29, 30 March 2008


PDB ID 1j5j

Drag the structure with the mouse to rotate
Related: 1LGL


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution structure of HERG-specific scorpion toxin BeKm-1


Overview

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.

About this Structure

1J5J is a Single protein structure of sequence from Mesobuthus eupeus. Full crystallographic information is available from OCA.

Reference

New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1., Korolkova YV, Bocharov EV, Angelo K, Maslennikov IV, Grinenko OV, Lipkin AV, Nosyreva ED, Pluzhnikov KA, Olesen SP, Arseniev AS, Grishin EV, J Biol Chem. 2002 Nov 8;277(45):43104-9. Epub 2002 Jul 31. PMID:12151390

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