title: Binding structure of the leucine aminopeptidase inhibitor microginin FR1.
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.
authors.affiliation: Institut für Biologie II, Microbiologie, Albert-Ludwigs-Universität, Schänzlestr. 1, D-79104 Freiburg im Breisgau, Germany.
authors.forename: Manuel
authors.initials: M
authors.lastname: Kraft
authors.forename: Christian
authors.initials: C
authors.lastname: Schleberger
authors.forename: Jürgen
authors.initials: J
authors.lastname: Weckesser
authors.forename: Georg E
authors.initials: GE
authors.lastname: Schulz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D018360:Crystallography, X-Ray; D007931:Leucyl Aminopeptidase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D046931:Microcystis / Q000737:chemistry; D008958:Models, Molecular; D011480:Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D011480:Protease Inhibitors; D007931:Leucyl Aminopeptidase