1lir
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1lir.gif|left|200px]] | + | [[Image:1lir.gif|left|200px]] |
| - | + | ||
| - | '''LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1lir |SIZE=350|CAPTION= <scene name='initialview01'>1lir</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LIR is a [ | + | 1LIR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10081954 10081954] |
[[Category: Leiurus quinquestriatus hebraeus]] | [[Category: Leiurus quinquestriatus hebraeus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: scorpion]] | [[Category: scorpion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:24 2008'' |
Revision as of 10:31, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:31:24 2008
