1lir

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lir OCA], [http://www.ebi.ac.uk/pdbsum/1lir PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lir RCSB]</span>
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'''LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES'''
'''LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES'''
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[[Category: Lu, Z.]]
[[Category: Lu, Z.]]
[[Category: Renisio, J G.]]
[[Category: Renisio, J G.]]
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[[Category: inward rectifier potassium channel]]
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[[Category: Inward rectifier potassium channel]]
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[[Category: neurotoxin]]
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[[Category: Neurotoxin]]
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[[Category: potassium channel blocker]]
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[[Category: Potassium channel blocker]]
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[[Category: scorpion]]
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[[Category: Scorpion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:18 2008''
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Revision as of 20:57, 2 May 2008

Template:STRUCTURE 1lir

LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES


Overview

Lq2 is a unique scorpion toxin. Acting from the extracellular side, Lq2 blocks the ion conduction pore in not only the voltage- and Ca2+ -activated channels, but also the inward-rectifier K+ channels. This finding argues that the three-dimensional structures of the pores in these K+ channels are similar. However, the amino acid sequences that form the external part of the pore are minimally conserved among the various classes of K+ channels. Because Lq2 can bind to all the three classes of K+ channels, we can use Lq2 as a structural probe to examine how the non-conserved pore-forming sequences are arranged in space to form similar pore structures. In the present study, we determined the three-dimensional structure of Lq2 using nuclear magnetic resonance (NMR) techniques. Lq2 consists of an alpha-helix (residues S10 to L20) and a beta-sheet, connected by an alphabeta3 loop (residues N22 to N24). The beta-sheet has two well-defined anti-parallel strands (residues G26 to M29 and residues K32 to C35), which are connected by a type I' beta-turn centered between residues N30 and K31. The N-terminal segment (residues Z1 to T8) appears to form a quasi-third strand of the beta-sheet.

About this Structure

1LIR is a Single protein structure of sequence from Leiurus quinquestriatus hebraeus. Full crystallographic information is available from OCA.

Reference

Solution structure of potassium channel-inhibiting scorpion toxin Lq2., Renisio JG, Lu Z, Blanc E, Jin W, Lewis JH, Bornet O, Darbon H, Proteins. 1999 Mar 1;34(4):417-26. PMID:10081954 Page seeded by OCA on Fri May 2 23:57:42 2008

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