ArticleMarine drugs2012
Atypical reactive center Kunitz-type inhibitor from the sea anemone Heteractis crispa.
Article in Marine drugs, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
- Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo.Marine drugs · 2024Article
- Venomics Reveals the Venom Complexity of Sea AnemoneMarine drugs · 2024Article
- Recombinant Analogs of Sea Anemone Kunitz-Type Peptides Influence P2X7 Receptor Activity in Neuro-2a Cells.Marine drugs · 2023Article
- Kunitz-Type Peptides from Sea Anemones Protect Neuronal Cells against Parkinson's Disease Inductors via Inhibition of ROS Production and ATP-Induced P2X7 Receptor Activation.International journal of molecular sciences · 2022Article
- AsKC11, a Kunitz Peptide fromMarine drugs · 2022Article
- Sea Anemone Kunitz-Type Peptides Demonstrate Neuroprotective Activity in the 6-Hydroxydopamine Induced Neurotoxicity Model.Biomedicines · 2021Article
- Kunitz-Type Peptides from the Sea AnemoneBiomedicines · 2020Article
- A new multigene HCIQ subfamily from the sea anemone Heteractis crispa encodes Kunitz-peptides exhibiting neuroprotective activity against 6-hydroxydopamine.Scientific reports · 2020Article
- Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea AnemoneMarine drugs · 2019Article
- Review
- Kunitz-Type Peptide HCRG21 from the Sea Anemone Heteractis crispa Is a Full Antagonist of the TRPV1 Receptor.Marine drugs · 2016Article
- The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels.Toxins · 2016Article
- New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispa.Marine drugs · 2015Article
- Ancient Venom Systems: A Review on Cnidaria Toxins.Toxins · 2015Review
- Analgesic effect of novel Kunitz-type polypeptides of the sea anemone Heteractis crispa.Doklady. Biochemistry and biophysics · 2015Article
- Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals.Marine drugs · 2013Review
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The primary structure of a new Kunitz-type protease inhibitor InhVJ from the sea anemone Heteractis crispa (Radianthus macrodactylus) was determined by protein sequencing and cDNA cloning. InhVJ amino acid sequence was shown to share high sequence identity (up to 98%) with the other known Kunitz-type sea anemones sequences. It was determined that the P1 Thr at the reactive site resulted in a decrease of the K(i) of InhVJ to trypsin and α-chymotrypsin (7.38 × 10(-8) M and 9.93 × 10(-7) M, respectively). By structure modeling the functional importance of amino acids at the reactive site as well as at the weak contact site were determined. The significant role of Glu45 for the orientation and stabilization of the InhVJ-trypsin complex was elucidated. We can suggest that there has been an adaptive evolution of the P1 residue at the inhibitor reactive site providing specialization or functional diversification of the paralogs. The appearance of a key so-called P1 Thr residue instead of Lys might lead to refinement of inhibitor specificity in the direction of subfamilies of serine proteases. The absence of Kv channel and TRPV1-receptor modulation activity was confirmed by electrophysiological screening tests.
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