The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides

@article{Knappe2010TheGR,
  title={The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides},
  author={T. Knappe and U. Linne and X. Xie and M. Marahiel},
  journal={FEBS Letters},
  year={2010},
  volume={584}
}
  • T. Knappe, U. Linne, +1 author M. Marahiel
  • Published 2010
  • Medicine, Chemistry
  • FEBS Letters
  • The glucagon receptor antagonist BI‐32169, recently isolated from Streptomyces sp., was described as a bicyclic peptide, although its primary structure comprises conserved elements of class I and class II lasso peptides. Tandem mass spectrometric and nuclear magnetic resonance spectroscopic studies revealed that BI‐32169 is a lasso‐structured peptide constituting the new class III of lasso peptides. The determined lasso fold opens new avenues to improve the promising biological activity of BI… CONTINUE READING

    Topics from this paper.

    High‐Resolution Crystal Structure of a Lasso Peptide
    • 28
    • Open Access
    The B1 Protein Guides the Biosynthesis of a Lasso Peptide
    • 20
    • Open Access

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 26 REFERENCES
    BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp.
    • 51
    Insights into the biosynthesis and stability of the lasso peptide capistruin.
    • 83
    • Open Access
    Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.
    • 174
    • Open Access