@article{2649, keywords = {Molecular Sequence Data, Bacteria, Models, Molecular, Protein Structure, Tertiary, Amino Acid Sequence, Sequence Alignment, Conserved Sequence, Protein Structure, Secondary, Protein Processing, Post-Translational, Bacteriocins, Biological Products, Peptides, PQQ Cofactor, Protein Sorting Signals}, author = {A James Link}, title = {Biosynthesis: Leading the way to RiPPs.}, abstract = {

Many peptide-based natural products require a leader peptide to reach their final modified form, but identifying 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.

}, year = {2015}, journal = {Nat Chem Biol}, volume = {11}, pages = {551-2}, month = {2015 Aug}, issn = {1552-4469}, doi = {10.1038/nchembio.1862}, language = {eng}, }