2006
DOI: 10.1016/j.febslet.2006.11.060
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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 Å resolution. The observed binding structure could be beneficial for the design of potent aminopeptidase inhibitors.

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Cited by 24 publications
(27 citation statements)
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“…The ppLAP-bestatin crystal structure showed excellent density for the bestatin inhibitor in the active site with bestatin, 11,18 and the bestatin derivative microginin FR1. 19 A schematic overview of the polar interactions of bestatin with ppLAP is given in Fig. 4.…”
Section: Structure Of Bestatin-bound Pplapmentioning
confidence: 99%
“…The ppLAP-bestatin crystal structure showed excellent density for the bestatin inhibitor in the active site with bestatin, 11,18 and the bestatin derivative microginin FR1. 19 A schematic overview of the polar interactions of bestatin with ppLAP is given in Fig. 4.…”
Section: Structure Of Bestatin-bound Pplapmentioning
confidence: 99%
“…This is common for all family 5 APNs. A role similar to that suggested for inactive proteases seems unlikely because aminopeptidase inhibitors have not been reported from plants, although aminopeptidase inhibitory peptides have been isolated from bacteria (Kraft et al ., 2006).…”
mentioning
confidence: 99%
“…The structure N-Me-Tyr-Tyr at the C-terminus seemed to be crucial for the inhibition of angiotensin-converting enzyme (ACE) (Ishida et al 2000). The inhibitory activity of some microginins for ACE was considered for the production of blood pressure-decreasing drugs (Kraft et al 2006). However, some microginins did not show any inhibition activity against trypsin, chymotrypsin, papain, elastase or protein phosphatase 1A (Ishida et al 1997).…”
Section: Discussionmentioning
confidence: 99%