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2lo7
From Proteopedia
(Difference between revisions)
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| - | + | ==Ts16 NMR solution structure== | |
| - | === | + | <StructureSection load='2lo7' size='340' side='right' caption='[[2lo7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| - | + | == 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> | |
| - | ==Function== | + | </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://www.rcsb.org/pdb/explore.do?structureId=2lo7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lo7 PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/TTX16_TITSE TTX16_TITSE]] Blocks potassium channels (By similarity).[UniProtKB:P0C183] | [[http://www.uniprot.org/uniprot/TTX16_TITSE TTX16_TITSE]] Blocks potassium channels (By similarity).[UniProtKB:P0C183] | ||
| + | <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> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Brazilian scorpion]] | [[Category: Brazilian scorpion]] | ||
| - | [[Category: Flores-Solis, D | + | [[Category: Flores-Solis, D]] |
| - | [[Category: Rio-Portilla, F del | + | [[Category: Rio-Portilla, F del]] |
| - | [[Category: Saucedo, A L | + | [[Category: Saucedo, A L]] |
[[Category: Alpha scorpion toxin]] | [[Category: Alpha scorpion toxin]] | ||
[[Category: Cs alpha alpha motif]] | [[Category: Cs alpha alpha motif]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
[[Category: Voltage gated potassium channel]] | [[Category: Voltage gated potassium channel]] | ||
Revision as of 08:48, 24 December 2014
Ts16 NMR solution structure
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