Binding structure of the leucine aminopeptidase inhibitor microginin FR1

FEBS Lett. 2006 Dec 22;580(30):6943-7. doi: 10.1016/j.febslet.2006.11.060. Epub 2006 Dec 4.

Abstract

Natural bioactive compounds are of general interest for pharmaceutical research because they may serve as leads in drug development campaigns. Among them, microginins are linear peptides known to inhibit various exopeptidases. The crystal structure of microginin FR1 from Microcystis sp. bound to bovine lens leucine aminopeptidase was established at 1.73 Angstrom resolution. The observed binding structure could be beneficial for the design of potent aminopeptidase inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Crystallography, X-Ray
  • Leucyl Aminopeptidase / antagonists & inhibitors
  • Leucyl Aminopeptidase / chemistry*
  • Leucyl Aminopeptidase / metabolism*
  • Microcystis / chemistry
  • Models, Molecular
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary

Substances

  • Protease Inhibitors
  • Leucyl Aminopeptidase