View source for 2mun


==Solution structure of mu-SLPTX3-Ssm6a==
<StructureSection load='2mun' size='340' side='right'caption='[[2mun]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scolopendra_subspinipes Scolopendra subspinipes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MUN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 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=2mun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mun OCA], [https://pdbe.org/2mun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mun RCSB], [https://www.ebi.ac.uk/pdbsum/2mun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TX32A_SCOMU TX32A_SCOMU] Gating-modifier toxin that inhibits voltage-gated sodium channel with a preference for hNav1.7/SCN9A (IC(50)=25.4 nM) over hNav1.1/SCN1A (IC(50)=4.1 uM), hNav1.2/SCN2A (IC(50)=813 nM), and hNav1.6/SCN8A (IC(50)=15.2 uM) (PubMed:24082113). Is an effective analgesic in rodent pain models, since it is several-fold more effective than morphine in a rodent model of formalin-induced pain and is equipotent with morphine in its ability to reduce thermal and acid-induced pain (PubMed:24082113). In addition, this peptide shows a high level of resistance to proteases and a high thermal stability that may be explained by its predominant composition of alpha-helices (PubMed:24082113).<ref>PMID:24082113</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal alpha helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution.

Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators.,Undheim EA, Grimm LL, Low CF, Morgenstern D, Herzig V, Zobel-Thropp P, Pineda SS, Habib R, Dziemborowicz S, Fry BG, Nicholson GM, Binford GJ, Mobli M, King GF Structure. 2015 Jun 2. pii: S0969-2126(15)00181-1. doi:, 10.1016/j.str.2015.05.003. PMID:26073605<ref>PMID:26073605</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mun" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Scolopendra subspinipes]]
[[Category: King GF]]
[[Category: Mobli M]]
[[Category: Undheim EAB]]