|
|
| (12 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1lir.gif|left|200px]] | |
| | | | |
| - | {{Structure
| + | ==LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES== |
| - | |PDB= 1lir |SIZE=350|CAPTION= <scene name='initialview01'>1lir</scene>
| + | <StructureSection load='1lir' size='340' side='right'caption='[[1lir]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1lir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LIR FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> |
| - | }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lir OCA], [https://pdbe.org/1lir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lir RCSB], [https://www.ebi.ac.uk/pdbsum/1lir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lir ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KAX12_LEIHE KAX12_LEIHE] Blocks calcium-activated potassium channels (Kd=43 nM on KCa1.1/KCNMA1). Has a potent presynaptic facilitatory action, with less effect on direct muscle stimulation.<ref>PMID:2477548</ref> <ref>PMID:7533951</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | 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. |
| | | | |
| - | '''LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES'''
| + | 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<ref>PMID:10081954</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1lir" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | 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.
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] |
| - | | + | == References == |
| - | ==About this Structure== | + | <references/> |
| - | 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].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference==
| + | [[Category: Large Structures]] |
| - | 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: Blanc E]] |
| - | [[Category: Blanc, E.]] | + | [[Category: Bornet O]] |
| - | [[Category: Bornet, O.]] | + | [[Category: Darbon H]] |
| - | [[Category: Darbon, H.]] | + | [[Category: Jin W]] |
| - | [[Category: Jin, W.]] | + | [[Category: Lewis JH]] |
| - | [[Category: Lewis, J H.]] | + | [[Category: Lu Z]] |
| - | [[Category: Lu, Z.]] | + | [[Category: Renisio JG]] |
| - | [[Category: Renisio, J G.]] | + | |
| - | [[Category: inward rectifier potassium channel]]
| + | |
| - | [[Category: neurotoxin]]
| + | |
| - | [[Category: potassium channel blocker]]
| + | |
| - | [[Category: scorpion]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:24 2008''
| + | |
| Structural highlights
Function
KAX12_LEIHE Blocks calcium-activated potassium channels (Kd=43 nM on KCa1.1/KCNMA1). Has a potent presynaptic facilitatory action, with less effect on direct muscle stimulation.[1] [2]
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lucchesi K, Ravindran A, Young H, Moczydlowski E. Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J Membr Biol. 1989 Aug;109(3):269-81. PMID:2477548 doi:10.1007/BF01870284
- ↑ Marshall DL, Vatanpour H, Harvey AL, Boyot P, Pinkasfeld S, Doljansky Y, Bouet F, Ménez A. Neuromuscular effects of some potassium channel blocking toxins from the venom of the scorpion Leiurus quinquestriatus hebreus. Toxicon. 1994 Nov;32(11):1433-43. PMID:7533951 doi:10.1016/0041-0101(94)90415-4
- ↑ Renisio JG, Lu Z, Blanc E, Jin W, Lewis JH, Bornet O, Darbon H. Solution structure of potassium channel-inhibiting scorpion toxin Lq2. Proteins. 1999 Mar 1;34(4):417-26. PMID:10081954
|
