2ndi: Difference between revisions

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'''Unreleased structure'''


The entry 2ndi is ON HOLD  until Paper Publication
==Solution structure of the toxin ISTX-I from Ixodes scapularis==
<StructureSection load='2ndi' size='340' side='right' caption='[[2ndi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ndi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black-legged_tick Black-legged tick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NDI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NDI 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=2ndi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ndi OCA], [http://pdbe.org/2ndi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ndi RCSB], [http://www.ebi.ac.uk/pdbsum/2ndi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ndi ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of arachnida, such as spiders and scorpions, commonly produce venom with specialized venom glands, paralyzing their prey with neurotoxins that specifically target ion channels. Two well-studied motifs, the disulfide-directed hairpin (DDH) and the inhibitor cystine knot motif (ICK), are both found in scorpion and spider toxins. As arachnids, ticks inject a neurotoxin-containing cocktail from their salivary glands into the host to acquire a blood meal, but peptide toxins acting on ion channels have not been observed in ticks. Here, a new neurotoxin (ISTX-I) that acts on sodium channels was identified from the hard tick Ixodes scapularis and characterized. ISTX-I exhibits a potent inhibitory function with an IC50 of 1.6 muM for sodium channel Nav1.7 but not other sodium channel subtypes. ISTX-I adopts a novel structural fold and is distinct from the canonical ICK motif. Analysis of the ISTX-I, DDH and ICK motifs reveals that the new ISTX-I motif might be an intermediate scaffold between DDH and ICK, and ISTX-I is a clue to the evolutionary link between the DDH and ICK motifs. These results provide a glimpse into the convergent evolution of neurotoxins from predatory and blood-sucking arthropods.


Authors: Hu, K.
A sodium channel inhibitor ISTX-I with a novel structure provides a new hint at the evolutionary link between two toxin folds.,Rong M, Liu J, Zhang M, Wang G, Zhao G, Wang G, Zhang Y, Hu K, Lai R Sci Rep. 2016 Jul 13;6:29691. doi: 10.1038/srep29691. PMID:27407029<ref>PMID:27407029</ref>


Description: Solution structure of the toxin ISTX-I from Ixodes scapularis
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 2ndi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Black-legged tick]]
[[Category: Hu, K]]
[[Category: Hu, K]]
[[Category: Toxin]]
[[Category: Toxin peptide]]
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