1lgl | pdb_00001lgl

Solution structure of HERG-specific scorpion toxin BeKm-1

spinqualitylabelsall models 1lgl, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lgl is a 1 chain structure with sequence from Mesobuthus eupeus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Potassium channel toxin

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