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- W2904897595 abstract "Disulfide-rich peptides (DRPs) play diverse physiological roles and have emerged as attractive sources of pharmacological tools and drug leads. Here we describe the 3D structure of a centipede venom peptide, U-SLPTX15-Sm2a, whose family defines a unique class of one of the most widespread DRP folds known, the cystine-stabilized α/β fold (CSαβ). This class, which we have named the two-disulfide CSαβ fold (2ds-CSαβ), contains only two internal disulfide bonds as opposed to at least three in all other confirmed CSαβ peptides, and constitutes one of the major neurotoxic peptide families in centipede venoms. We show the 2ds-CSαβ is widely distributed outside centipedes and is likely an ancient fold predating the split between prokaryotes and eukaryotes. Our results provide insights into the ancient evolutionary history of a widespread DRP fold and highlight the usefulness of 3D structures as evolutionary tools." @default.
- W2904897595 created "2018-12-22" @default.
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- W2904897595 date "2019-02-01" @default.
- W2904897595 modified "2023-10-17" @default.
- W2904897595 title "A Centipede Toxin Family Defines an Ancient Class of CSαβ Defensins" @default.
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- W2904897595 doi "https://doi.org/10.1016/j.str.2018.10.022" @default.
- W2904897595 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30554841" @default.
- W2904897595 hasPublicationYear "2019" @default.
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