View source for 5we3


==Solution NMR structure of PaurTx-3==
<StructureSection load='5we3' size='340' side='right'caption='[[5we3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5we3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraphysa_scrofa Paraphysa scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WE3 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=5we3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5we3 OCA], [https://pdbe.org/5we3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5we3 RCSB], [https://www.ebi.ac.uk/pdbsum/5we3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5we3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TX3_PARSR TX3_PARSR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spider gating modifier toxins (GMTs) are potent modulators of voltage-gated ion channels and have thus attracted attention as drug leads for several pathophysiological conditions. GMTs contain three disulfide bonds organized in an inhibitory cystine knot, which putatively confers them with high stability; however, thus far, there has not been a focused study to establish the stability of GMTs in physiological conditions. We examined the resistance of five GMTs including GpTx-1, HnTx-IV, HwTx-IV, PaurTx-3 and SgTx-1, to pH, thermal and proteolytic degradation. The peptides were stable under physiological conditions, except SgTx-1, which was susceptible to proteolysis, probably due to a longer C-terminus compared to the other peptides. In non-physiological conditions, the five peptides withstood chaotropic degradation, and all but SgTx-1 remained intact after prolonged exposure to high temperature; however, the peptides were degraded in strongly alkaline solutions. GpTx-1 and PaurTx-3 were more resistant to basic hydrolysis than HnTx-IV, HwTx-IV and SgTx-1, probably because a shorter interconnecting loop 3 on GpTx-1 and PaurTx-3 may stabilize interactions between the C-terminus and the hydrophobic patch. Here, we establish that most GMTs are exceptionally stable, and propose that, in the design of GMT-based therapeutics, stability can be enhanced by optimizing the C-terminus in terms of length, and increased interactions with the hydrophobic patch.

Lengths of the C-Terminus and Interconnecting Loops Impact Stability of Spider-Derived Gating Modifier Toxins.,Agwa AJ, Huang YH, Craik DJ, Henriques ST, Schroeder CI Toxins (Basel). 2017 Aug 12;9(8). pii: E248. doi: 10.3390/toxins9080248. PMID:28805686<ref>PMID:28805686</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5we3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paraphysa scrofa]]
[[Category: Agwa AJ]]
[[Category: Schroeder CI]]