ArticleProceedings of the National Academy of Sciences of the United States of America2011
Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 100 citations in OpenAlex.
- Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.Chemical science · 2025Review
- Properties and Pharmacology of Scorpion Toxins and Their Biotechnological Potential in Agriculture and Medicine.Toxins · 2025Review
- Structural analysis of an Asterias rubens peptide indicates the presence of a disulfide-directed β-hairpin fold.FEBS open bio · 2025Article
- Triscysteine disulfide-directing motifs enabling design and discovery of multicyclic peptide binders.Nature communications · 2024Article
- Two Novel Mosquitocidal Peptides Isolated from the Venom of the Bahia Scarlet Tarantula (Toxins · 2023Article
- Article
- Structure-guided design of CPPC-paired disulfide-rich peptide libraries for ligand and drug discovery.Chemical science · 2022Article
- Structural and Functional Diversity of Animal Toxins Interacting With GPCRs.Frontiers in molecular biosciences · 2022Review
- An evolution-inspired strategy to design disulfide-rich peptides tolerant to extensive sequence manipulation.Chemical science · 2021Article
- Small Molecules in the Venom of the ScorpionBiomedicines · 2020Article
- Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Scorpion Venom: Detriments and Benefits.Biomedicines · 2020Review
- Australian ScorpionBiomolecules · 2020Article
- Venom Peptides with Dual Modulatory Activity on the Voltage-Gated Sodium Channel NaACS pharmacology & translational science · 2020Article
- Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the ScorpionMolecules (Basel, Switzerland) · 2018Article
- PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold.Cellular and molecular life sciences : CMLS · 2018Article
- Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid ScorpionToxins · 2018Article
- An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches.PloS one · 2018Article
- Review
- Joannsin, a novel Kunitz-type FXa inhibitor from the venom of Prospirobolus joannsi.Thrombosis and haemostasis · 2017Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three-disulfide inhibitor cystine knot (ICK) motif is a fold common to venom peptides from spiders, scorpions, and aquatic cone snails. Over a decade ago it was proposed that the ICK motif is an elaboration of an ancestral two-disulfide fold coined the disulfide-directed β-hairpin (DDH). Here we report the isolation, characterization, and structure of a novel toxin [U(1)-liotoxin-Lw1a (U(1)-LITX-Lw1a)] from the venom of the scorpion Liocheles waigiensis that is the first example of a native peptide that adopts the DDH fold. U(1)-LITX-Lw1a not only represents the discovery of a missing link in venom protein evolution, it is the first member of a fourth structural fold to be adopted by scorpion-venom peptides. Additionally, we show that U(1)-LITX-Lw1a has potent insecticidal activity across a broad range of insect pest species, thereby providing a unique structural scaffold for bioinsecticide development.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.