Many peptide-based natural products require a leader peptide to reach their final modified form, but the identification of general rules for leader peptide interactions have been stymied by the diversity of these molecules. Two papers reporting crystallographic and bioinformatic analysis of these systems now reveal a structurally conserved domain that mediates leader peptide binding.
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The author declares no competing financial interests.
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Link, A. Leading the way to RiPPs. Nat Chem Biol 11, 551–552 (2015). https://doi.org/10.1038/nchembio.1862
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