1lir

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[[Image:1lir.png|left|200px]]
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==LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES==
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<StructureSection load='1lir' size='340' side='right' caption='[[1lir]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lir]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LIR FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1lir RCSB], [http://www.ebi.ac.uk/pdbsum/1lir PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1lir| PDB=1lir | SCENE= }}
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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>
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===LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_10081954}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1lir]] is a 1 chain structure with sequence from [http://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].
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</StructureSection>
[[Category: Leiurus quinquestriatus hebraeus]]
[[Category: Leiurus quinquestriatus hebraeus]]
[[Category: Blanc, E.]]
[[Category: Blanc, E.]]

Revision as of 17:53, 28 September 2014

LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES

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