6vh8
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==NMR Solution Structure of Excelsatoxin A== | |
+ | <StructureSection load='6vh8' size='340' side='right'caption='[[6vh8]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VH8 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=6vh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vh8 OCA], [https://pdbe.org/6vh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vh8 RCSB], [https://www.ebi.ac.uk/pdbsum/6vh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vh8 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Stinging trees from Australasia produce remarkably persistent and painful stings upon contact of their stiff epidermal hairs, called trichomes, with mammalian skin. Dendrocnide-induced acute pain typically lasts for several hours, and intermittent painful flares can persist for days and weeks. Pharmacological activity has been attributed to small-molecule neurotransmitters and inflammatory mediators, but these compounds alone cannot explain the observed sensory effects. We show here that the venoms of Australian Dendrocnide species contain heretofore unknown pain-inducing peptides that potently activate mouse sensory neurons and delay inactivation of voltage-gated sodium channels. These neurotoxins localize specifically to the stinging hairs and are miniproteins of 4 kDa, whose 3D structure is stabilized in an inhibitory cystine knot motif, a characteristic shared with neurotoxins found in spider and cone snail venoms. Our results provide an intriguing example of inter-kingdom convergent evolution of animal and plant venoms with shared modes of delivery, molecular structure, and pharmacology. | ||
- | + | Neurotoxic peptides from the venom of the giant Australian stinging tree.,Gilding EK, Jami S, Deuis JR, Israel MR, Harvey PJ, Poth AG, Rehm FBH, Stow JL, Robinson SD, Yap K, Brown DL, Hamilton BR, Andersson D, Craik DJ, Vetter I, Durek T Sci Adv. 2020 Sep 16;6(38). pii: 6/38/eabb8828. doi: 10.1126/sciadv.abb8828., Print 2020 Sep. PMID:32938666<ref>PMID:32938666</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Craik | + | <div class="pdbe-citations 6vh8" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Craik DJ]] | ||
+ | [[Category: Durek T]] | ||
+ | [[Category: Harvey PJ]] |
Current revision
NMR Solution Structure of Excelsatoxin A
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