1j5j: Difference between revisions

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[[Image:1j5j.jpg|left|200px]]
[[Image:1j5j.jpg|left|200px]]


{{Structure
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|RELATEDENTRY=[[1lgl|1LGL]]
|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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'''Solution structure of HERG-specific scorpion toxin BeKm-1'''
'''Solution structure of HERG-specific scorpion toxin BeKm-1'''
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[[Category: Olesen, S P.]]
[[Category: Olesen, S P.]]
[[Category: Pluzhnikov, K A.]]
[[Category: Pluzhnikov, K A.]]
[[Category: alpha-beta motif]]
[[Category: Alpha-beta motif]]
[[Category: cysteine-knot motif]]
[[Category: Cysteine-knot motif]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:49:54 2008''
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Revision as of 20:49, 2 May 2008

File:1j5j.jpg

Template:STRUCTURE 1j5j

Solution structure of HERG-specific scorpion toxin BeKm-1


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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 Page seeded by OCA on Fri May 2 20:49:54 2008

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