ArticleThe FEBS journal2018
Structural plasticity of mini-M conotoxins - expression of all mini-M subtypes by Conus regius.
Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Profiling the Paralytic Effects and Lethality of Cone Snail Venom Toxins Using Nanofractionation Analytics withToxins · 2025Article
- An Orthogonal Protection Strategy for the Synthesis of Conotoxins Containing Three Disulfide Bonds.Marine drugs · 2025Article
- Cone snail species off the Brazilian coast and their venoms: a review and update.The journal of venomous animals and toxins including tropical diseases · 2023Review
- Review
- Synthesis and Characterization of an Analgesic Potential Conotoxin Lv32.1.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
6 authors.
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Abstract
The mini-M conotoxins are peptidic scaffolds found in the venom of cones snails. These scaffolds are tightly folded structures held together by three disulfide bonds with a CC-C-C-CC arrangement (conotoxin framework III) and belong to the M Superfamily of conotoxins. Here, we describe mini-M conotoxins from the venom of Conus regius, a Western Atlantic worm-hunting cone snail species using transcriptomic and peptidomic analyses. These C. regius conotoxins belong to three different subtypes: M1, M2, and M3. The subtypes show little sequence homology, and their loop sizes (intercysteine amino acid chains) vary significantly. The mini-Ms isolated from dissected venom contains preferentially hydroxylated proline residues, thus augmenting the structural reach of this conotoxin class. Using 2D-NMR methods, we have determined the 3D structure of reg3b, an M2 subtype conotoxin, which shows a constrained multi-turn scaffold. The structural diversity found within mini-M conotoxin scaffolds of C. regius is indicative of structural hypervariability of the conotoxin M superfamily that is not seen in other superfamilies. These stable minimalistic scaffolds may be investigated for the development of engineered peptides for therapeutic applications. DATABASES: Sequences are available in GenBank under accession numbers MF588935-MF588952. Structural data are available in the RCSB protein database under the accession code 6BX9.
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