2li3: Difference between revisions
New page: '''Unreleased structure''' The entry 2li3 is ON HOLD Authors: Saucedo-Yanez, A., Del Rio-Portilla, F., Hernandez-Lopez, R. Description: Structural and functional analysis of a novel po... |
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==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]] | |||
Latest revision as of 09:10, 27 November 2024
Structural and functional analysis of a novel potassium toxin argentinean scorpion Tityus trivittatus reveals a new kappa sub-familyStructural and functional analysis of a novel potassium toxin argentinean scorpion Tityus trivittatus reveals a new kappa sub-family
Structural highlights
Publication Abstract from PubMedScorpion 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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