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| | ==Ts16 NMR solution structure== | | ==Ts16 NMR solution structure== |
| - | <StructureSection load='2lo7' size='340' side='right' caption='[[2lo7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lo7' size='340' side='right'caption='[[2lo7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lo7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brazilian_scorpion Brazilian scorpion]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2lka 2lka]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LO7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lo7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2lka 2lka]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LO7 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=2lo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lo7 OCA], [http://pdbe.org/2lo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lo7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lo7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lo7 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lo7 OCA], [https://pdbe.org/2lo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lo7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lo7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TTX16_TITSE TTX16_TITSE]] Blocks potassium channels (By similarity).[UniProtKB:P0C183] | + | [https://www.uniprot.org/uniprot/KA20_TITSE KA20_TITSE] Blocks potassium channels.[UniProtKB:P0C183] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brazilian scorpion]] | + | [[Category: Large Structures]] |
| - | [[Category: Flores-Solis, D]] | + | [[Category: Tityus serrulatus]] |
| - | [[Category: Rio-Portilla, F del]] | + | [[Category: Flores-Solis D]] |
| - | [[Category: Saucedo, A L]] | + | [[Category: Saucedo AL]] |
| - | [[Category: Alpha scorpion toxin]] | + | [[Category: Del Rio-Portilla F]] |
| - | [[Category: Cs alpha alpha motif]]
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| - | [[Category: Toxin]]
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| - | [[Category: Voltage gated potassium channel]]
| + | |
| Structural highlights
Function
KA20_TITSE Blocks potassium channels.[UniProtKB:P0C183]
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.
References
- ↑ 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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