2li3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural and functional analysis of a novel potassium toxin argentinean scorpion Tityus trivittatus reveals a new kappa sub-family== | |
| + | <StructureSection load='2li3' size='340' side='right'caption='[[2li3]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2li3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tityus_trivittatus Tityus trivittatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LI3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2li3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li3 OCA], [https://pdbe.org/2li3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2li3 RCSB], [https://www.ebi.ac.uk/pdbsum/2li3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2li3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Scorpion venoms are a rich source of K(+) channel-blocking peptides. For the most part, they are structurally related small disulfide-rich proteins containing a conserved pattern of six cysteines that is assumed to dictate their common three-dimensional folding. In the conventional pattern, two disulfide bridges connect an alpha-helical segment to the C-terminal strand of a double- or triple-stranded beta-sheet, conforming a cystine-stabilized alpha/beta scaffold (CSalpha/beta). Here we show that two K(+) channel-blocking peptides from Tityus scorpions conserve the cysteine spacing of common scorpion venom peptides but display an unconventional disulfide pattern, accompanied by a complete rearrangement of the secondary structure topology into a CS helix-loop-helix fold. Sequence and structural comparisons of the peptides adopting this novel fold suggest that it would be a new elaboration of the widespread CSalpha/beta scaffold, thus revealing an unexpected structural versatility of these small disulfide-rich proteins. Acknowledgment of such versatility is important to understand how venom structural complexity emerged on a limited number of molecular scaffolds. | ||
| - | + | New Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACING.,Saucedo AL, Flores-Solis D, Rodriguez de la Vega RC, Ramirez-Cordero B, Hernandez-Lopez R, Cano-Sanchez P, Navarro RN, Garcia-Valdes J, Coronas-Valderrama F, de Roodt A, Brieba LG, Possani LD, Del Rio-Portilla F J Biol Chem. 2012 Apr 6;287(15):12321-30. Epub 2012 Jan 10. PMID:22238341<ref>PMID:22238341</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2li3" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tityus trivittatus]] | ||
| + | [[Category: Del Rio-Portilla F]] | ||
| + | [[Category: Hernandez-Lopez R]] | ||
| + | [[Category: Saucedo-Yanez A]] | ||
Current revision
Structural and functional analysis of a novel potassium toxin argentinean scorpion Tityus trivittatus reveals a new kappa sub-family
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