ArticlePloS one2012
Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Effects of Cape Cobra (Toxins · 2026Article
- Review
- Differential effects of the venoms of Russell's viper and Indian cobra on human myoblasts.Scientific reports · 2024Article
- Immunogenic potential and neutralizing ability of a heterologous version of the most abundant three-finger toxin from the coral snakeThe journal of venomous animals and toxins including tropical diseases · 2024Article
- Snake Venom Components as Therapeutic Drugs in Ischemic Heart Disease.Biomolecules · 2023Review
- Unveiling the functional epitopes of cobra venom cytotoxin by immunoinformatics and epitope-omic analyses.Scientific reports · 2023Article
- Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases.Molecules (Basel, Switzerland) · 2021Review
- Effects of 3FTx Protein Fraction fromMolecules (Basel, Switzerland) · 2021Article
- Article
- Isolation and characterization of cytotoxic and insulin-releasing components from the venom of the black-necked spitting cobraToxicon: X · 2020Article
- Snake Venom Peptides: Tools of Biodiscovery.Toxins · 2018Review
- Ringhalexin from Hemachatus haemachatus: A novel inhibitor of extrinsic tenase complex.Scientific reports · 2016Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Snake venoms are rich sources of biologically active proteins and polypeptides. Three-finger toxins are non-enzymatic proteins present in elapid (cobras, kraits, mambas and sea snakes) and colubrid venoms. These proteins contain four conserved disulfide bonds in the core to maintain the three-finger folds. Although all three-finger toxins have similar fold, their biological activities are different. A new three-finger toxin (hemachatoxin) was isolated from Hemachatus haemachatus (Ringhals cobra) venom. Its amino acid sequence was elucidated, and crystal structure was determined at 2.43 Å resolution. The overall fold is similar to other three-finger toxins. The structure and sequence analysis revealed that the fold is maintained by four highly conserved disulfide bonds. It exhibited highest similarity to particularly P-type cardiotoxins that are known to associate and perturb the membrane surface with their lipid binding sites. Also, the increased B value of hemachotoxin loop II suggests that loop II is flexible and may remain flexible until its interaction with membrane phospholipids. Based on the analysis, we predict hemachatoxin to be cardiotoxic/cytotoxic and our future experiments will be directed to characterize the activity of hemachatoxin.
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