2me7: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "2me7" [edit=sysop:move=sysop] |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==NMR solution structure of the GS-TAMAPIN MUTATION R6A== | ||
<StructureSection load='2me7' size='340' side='right'caption='[[2me7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2me7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_tamulus Mesobuthus tamulus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ME7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ME7 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=2me7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2me7 OCA], [https://pdbe.org/2me7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2me7 RCSB], [https://www.ebi.ac.uk/pdbsum/2me7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2me7 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The scorpion toxin tamapin displays the most potent and selective blockage against KCa2.2 channels known to date. In this work, we report the biosynthesis, three-dimensional structure, and cytotoxicity on cancer cell lines (Jurkat E6-1 and human mammary breast cancer MDA-MB-231) of recombinant tamapin and five related peptides bearing mutations on residues (R6A,R7A, R13A, R6A-R7A, and GS-tamapin) that were previously suggested to be important for tamapin's activity. The indicated cell lines were used as they constitutively express KCa2.2 channels. The studied toxin-like peptides displayed lethal responses on Jurkat T cells and breast cancer cells; their effect is dose- and time-dependent with IC50 values in the nanomolar range. The order of potency is r-tamapin > GS-tamapin > R6A > R13A > R6A-R7A > R7A for Jurkat T cells and r-tamapin > R7A for MDA-MB-231 breast cancer cells. Our structural determination by NMR demonstrated that r-tamapin preserves the folding of the alphaKTx5 subfamily and that neither single nor double alanine mutations affect the three-dimensional structure of the wild-type peptide. In contrast, our activity assays show that changes in cytotoxicity are related to the chemical nature of certain residues. Our results suggest that the toxic activity of r-tamapin on Jurkat and breast cancer cells could be mediated by the interaction of charged residues in tamapin with KCa2.2 channels via the apoptotic cell death pathway. | |||
Cytotoxicity of Recombinant Tamapin and Related Toxin-Like Peptides on Model Cell Lines.,Ramirez-Cordero B, Toledano Y, Cano-Sanchez P, Hernandez-Lopez R, Flores-Solis D, Saucedo-Yanez AL, Chavez-Uribe I, Brieba LG, Del Rio-Portilla F Chem Res Toxicol. 2014 May 12. PMID:24821061<ref>PMID:24821061</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2me7" 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: Mesobuthus tamulus]] | |||
[[Category: Ramirez-Cordero B]] | |||
[[Category: Del Rio-Portilla F]] | |||
Latest revision as of 01:11, 21 November 2024
NMR solution structure of the GS-TAMAPIN MUTATION R6A
| ||||||||||||
