6VH8

NMR Solution Structure of Excelsatoxin A

Summary for 6VH8

• Entry DOI: 10.2210/pdb6vh8/pdb
• NMR Information: BMRB: 30711
• Descriptor: Excelsatoxin A (1 entity in total)
• Functional Keywords: ick peptide, inhibitor cystine knot, plant toxin, toxin
• Biological source: Dendrocnide excelsa
• Total number of polymer chains: 1
• Total formula weight: 3888.71

Authors

Harvey, P.J.,Durek, T.,Craik, D.J. (deposition date: 2020-01-09, release date: 2020-09-30, Last modification date: 2024-11-20)

Primary citation

Gilding, E.K.,Jami, S.,Deuis, J.R.,Israel, M.R.,Harvey, P.J.,Poth, A.G.,Rehm, F.B.H.,Stow, J.L.,Robinson, S.D.,Yap, K.,Brown, D.L.,Hamilton, B.R.,Andersson, D.,Craik, D.J.,Vetter, I.,Durek, T.
Neurotoxic peptides from the venom of the giant Australian stinging tree.
Sci Adv, 6:-, 2020

PubMed Abstract: Stinging trees from Australasia produce remarkably persistent and painful stings upon contact of their stiff epidermal hairs, called trichomes, with mammalian skin. -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 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.

PubMed: 32938666
DOI: 10.1126/sciadv.abb8828

Experimental method

SOLUTION NMR