7JPM
The solution structure of omega-theraphotoxin-Pm1b isolated from King Baboon spider
Summary for 7JPM
| Entry DOI | 10.2210/pdb7jpm/pdb |
| NMR Information | BMRB: 30785 |
| Descriptor | Omega-theraphotoxin-Pm1b (1 entity in total) |
| Functional Keywords | inhibitor, cystein knot, voltage-gated sodium channel modulator, toxin |
| Biological source | Pelinobius muticus (king baboon spider) |
| Total number of polymer chains | 1 |
| Total formula weight | 4541.07 |
| Authors | Chin, Y.K.-Y.,Ziegman, R.,Alewood, P.F. (deposition date: 2020-08-09, release date: 2021-09-08, Last modification date: 2024-10-23) |
| Primary citation | Finol-Urdaneta, R.K.,Ziegman, R.,Dekan, Z.,McArthur, J.R.,Heitmann, S.,Luna-Ramirez, K.,Tae, H.S.,Mueller, A.,Starobova, H.,Chin, Y.K.,Wingerd, J.S.,Undheim, E.A.B.,Cristofori-Armstrong, B.,Hill, A.P.,Herzig, V.,King, G.F.,Vetter, I.,Rash, L.D.,Adams, D.J.,Alewood, P.F. Multitarget nociceptor sensitization by a promiscuous peptide from the venom of the King Baboon spider. Proc.Natl.Acad.Sci.USA, 119:-, 2022 Cited by PubMed Abstract: The King Baboon spider, , is a burrowing African tarantula. Its impressive size and appealing coloration are tempered by reports describing severe localized pain, swelling, itchiness, and muscle cramping after accidental envenomation. Hyperalgesia is the most prominent symptom after bites from , but the molecular basis by which the venom induces pain is unknown. Proteotranscriptomic analysis of venom uncovered a cysteine-rich peptide, δ/κ-theraphotoxin-Pm1a (δ/κ-TRTX-Pm1a), that elicited nocifensive behavior when injected into mice. In small dorsal root ganglion neurons, synthetic δ/κ-TRTX-Pm1a (sPm1a) induced hyperexcitability by enhancing tetrodotoxin-resistant sodium currents, impairing repolarization and lowering the threshold of action potential firing, consistent with the severe pain associated with envenomation. The molecular mechanism of nociceptor sensitization by sPm1a involves multimodal actions over several ion channel targets, including Na1.8, K2.1, and tetrodotoxin-sensitive Na channels. The promiscuous targeting of peptides like δ/κ-TRTX-Pm1a may be an evolutionary adaptation in pain-inducing defensive venoms. PubMed: 35074873DOI: 10.1073/pnas.2110932119 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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