2li3: Difference between revisions

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<StructureSection load='2li3' size='340' side='right' caption='[[2li3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2li3' size='340' side='right' caption='[[2li3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2li3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LI3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2li3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Argentinean_scorpion Argentinean scorpion]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LI3 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2li3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2li3 RCSB], [http://www.ebi.ac.uk/pdbsum/2li3 PDBsum]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2li3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li3 OCA], [http://pdbe.org/2li3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2li3 RCSB], [http://www.ebi.ac.uk/pdbsum/2li3 PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2li3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Tityus trivittatus]]
[[Category: Argentinean scorpion]]
[[Category: Hernandez-Lopez, R]]
[[Category: Hernandez-Lopez, R]]
[[Category: Rio-Portilla, F Del]]
[[Category: Rio-Portilla, F Del]]

Revision as of 05:07, 11 September 2015

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

2li3 is a 1 chain structure with sequence from Argentinean scorpion. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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. New Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACING. J Biol Chem. 2012 Apr 6;287(15):12321-30. Epub 2012 Jan 10. PMID:22238341 doi:10.1074/jbc.M111.329607
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