2N6R
NMR structure of spider toxin U4-hexatoxin-Hi1a
Summary for 2N6R
| Entry DOI | 10.2210/pdb2n6r/pdb |
| NMR Information | BMRB: 25778 |
| Descriptor | U4-hexatoxin-Hi1a (1 entity in total) |
| Functional Keywords | spider toxin, inhibitor cystine knot, toxin |
| Biological source | Hadronyche infensa |
| Total number of polymer chains | 1 |
| Total formula weight | 8821.94 |
| Authors | Pineda, S.S.,Chin, Y.K.-Y.,King, G.F. (deposition date: 2015-08-28, release date: 2016-08-31, Last modification date: 2024-10-30) |
| Primary citation | Pineda, S.S.,Chin, Y.K.,Undheim, E.A.B.,Senff, S.,Mobli, M.,Dauly, C.,Escoubas, P.,Nicholson, G.M.,Kaas, Q.,Guo, S.,Herzig, V.,Mattick, J.S.,King, G.F. Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene. Proc.Natl.Acad.Sci.USA, 117:11399-11408, 2020 Cited by PubMed Abstract: Spiders are one of the most successful venomous animals, with more than 48,000 described species. Most spider venoms are dominated by cysteine-rich peptides with a diverse range of pharmacological activities. Some spider venoms contain thousands of unique peptides, but little is known about the mechanisms used to generate such complex chemical arsenals. We used an integrated transcriptomic, proteomic, and structural biology approach to demonstrate that the lethal Australian funnel-web spider produces 33 superfamilies of venom peptides and proteins. Twenty-six of the 33 superfamilies are disulfide-rich peptides, and we show that 15 of these are knottins that contribute >90% of the venom proteome. NMR analyses revealed that most of these disulfide-rich peptides are structurally related and range in complexity from simple to highly elaborated knottin domains, as well as double-knot toxins, that likely evolved from a single ancestral toxin gene. PubMed: 32398368DOI: 10.1073/pnas.1914536117 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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