Structural plasticity of mini‐M conotoxins – expression of all mini‐M subtypes by <i>Conus regius</i>

Franco, Aldo; Dovell, Sanaz; Möller, Carolina; Grandal, Meghan; Clark, E. P.; Marí, Frank

doi:10.1111/febs.14372

Cited by 9 publications

(15 citation statements)

References 53 publications

(67 reference statements)

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“…Different disulfide connectivity had been reported between and within the sub-branch conotoxins . The subtypes show little sequence homology, and their loop sizes vary …”

Section: Integrated Venomicsmentioning

confidence: 99%

“…88 The subtypes show little sequence homology, and their loop sizes vary. 86 3.4.4. Framework IV, CC−C−C−C−C.…”

Section: New Sequencesmentioning

confidence: 99%

“…Framework III conotoxin reg3b has the same connectivity as ar1446 and μ-BtIIIA, but it folds differently. 86 Its structure was described as a constrained multiturn scaffold, and we have classified it as fold N (Figure 30). Conotoxins displaying the same framework and connectivity can therefore fold differently.…”

Section: Structures Of Framework With Six Cysteinesmentioning

confidence: 99%

“…μ-Conotoxins have been very valuable tools to study sodium channel subtypes. − Ten μ-conotoxins have been discovered/revisited during the last five years, including μ-Mi040, μ-SmIIIA, μ-SIIIA, μ-GIIIA, μ-PIIIA, μ-SxIIIA, μ-BuIIIB, μ-Vx3-VV01, μ-reg3b, and μ-KIIIA. Depending on the number of residues located in the last loop (between Cys4 and Cys5), this framework has been divided into sub-branches, namely M-1, -2, -3, and -4 (Figure ).…”

Section: Integrated Venomicsmentioning

confidence: 99%

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Conotoxins: Chemistry and Biology

et al. 2019

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The venom of the marine predatory cone snails (genus Conus) has evolved for prey capture and defense, providing the basis for survival and rapid diversification of the now estimated 750+ species. A typical Conus venom contains hundreds to thousands of bioactive peptides known as conotoxins. These mostly disulfide-rich and well-structured peptides act on a wide range of targets such as ion channels, G protein-coupled receptors, transporters, and enzymes. Conotoxins are of interest to neuroscientists as well as drug developers due to their exquisite potency and selectivity, not just against prey but also mammalian targets, thereby providing a rich source of molecular probes and therapeutic leads. The rise of integrated venomics has accelerated conotoxin discovery with now well over 10,000 conotoxin sequences published. However, their structural and pharmacological characterization lags considerably behind. In this review, we highlight the diversity of new conotoxins uncovered since 2014, their three-dimensional structures and folds, novel chemical approaches to their syntheses, and their value as pharmacological tools to unravel complex biology. Additionally, we discuss challenges and future directions for the field.

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“…Different disulfide connectivity had been reported between and within the sub-branch conotoxins . The subtypes show little sequence homology, and their loop sizes vary …”

Section: Integrated Venomicsmentioning

confidence: 99%

“…88 The subtypes show little sequence homology, and their loop sizes vary. 86 3.4.4. Framework IV, CC−C−C−C−C.…”

Section: New Sequencesmentioning

confidence: 99%

Section: Structures Of Framework With Six Cysteinesmentioning

confidence: 99%

Section: Integrated Venomicsmentioning

confidence: 99%

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Conotoxins: Chemistry and Biology

et al. 2019

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“…Another curious finding within cluster 1 was the presence of mini-M conotoxins PIIIG, PIIIH, and PIII-I. While these conotoxins are prevalent in worm and mollusk-hunting Conus species ( 54 , 55 ), they have not been found in the injected venom of fish hunting species until now. The significance of this finding is under investigation.…”

Section: Discussionmentioning

confidence: 99%

Proteogenomic Assessment of Intraspecific Venom Variability: Molecular Adaptations in the Venom Arsenal of Conus purpurascens

Grandal

Hoggard

Neely

et al. 2021

Molecular & Cellular Proteomics

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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A short framework-III (mini-M-2) conotoxin from the venom of a vermivorous species, Conus archon, inhibits human neuronal nicotinic acetylcholine receptors

et al. 2022

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Structural plasticity of mini‐M conotoxins – expression of all mini‐M subtypes by Conus regius

Abstract: Sequences are available in GenBank under accession numbers MF588935-MF588952. Structural data are available in the RCSB protein database under the accession code 6BX9.

Cited by 9 publications

References 53 publications

Conotoxins: Chemistry and Biology

Conotoxins: Chemistry and Biology

Proteogenomic Assessment of Intraspecific Venom Variability: Molecular Adaptations in the Venom Arsenal of Conus purpurascens

A short framework-III (mini-M-2) conotoxin from the venom of a vermivorous species, Conus archon, inhibits human neuronal nicotinic acetylcholine receptors

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