ArticleProtein science : a publication of the Protein Society2003
Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 43 citations in OpenAlex.
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- Venomics and Peptidomics of Palearctic Vipers: A Clade-Wide Analysis of Seven Taxa of the GeneraJournal of proteome research · 2024Article
- RETRACTED: Structure-Activity Relationship of Synthetic Linear KTS-Peptides Containing Meta-Aminobenzoic Acid as Antagonists of α1β1 Integrin with Anti-Angiogenic and Melanoma Anti-Tumor Activities.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Novel contact-kinin inhibitor sylvestin targets thromboinflammation and ameliorates ischemic stroke.Cellular and molecular life sciences : CMLS · 2022Article
- Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction.Frontiers in molecular biosciences · 2021Review
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- Ndr2 Kinase Controls Neurite Outgrowth and Dendritic Branching Through αFrontiers in molecular neuroscience · 2018Article
- Review
- Anti-metastatic activity of the recombinant disintegrin, r-mojastin 1, from the Mohave rattlesnake.Toxicon : official journal of the International Society on Toxinology · 2011Article
- Snake venom disintegrins and cell migration.Toxins · 2010Review
- Cloning, expression, and hemostatic activities of a disintegrin, r-mojastin 1, from the mohave rattlesnake (Crotalus scutulatus scutulatus).Thrombosis research · 2010Article
- Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: insight into the evolution of the snake venom integrin-inhibition system.The Biochemical journal · 2006Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disintegrins represent a group of cysteine-rich peptides occurring in Crotalidae and Viperidae snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the Vipera lebetina obtusa viper, and represents the first potent and selective inhibitor of the binding of integrin alpha(1)beta(1) to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin-binding loop of obtustatin is two residues shorter and does not express the classical RGD sequence. Using synthetic peptides, a KTS motif was identified as the integrin-binding sequence. A three-dimensional model of obtustatin, built by homology-modeling structure calculations using different templates and alignments, strongly indicates that the novel KTS motif may reside at the tip of a flexible loop.
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