2j9a

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2j9a, resolution 1.73Å

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BLLAP IN COMPLEX WITH MICROGININ FR1

Overview

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.

About this Structure

2J9A is a Single protein structure of sequence from Bos taurus and Microcystis sp. with , , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Binding structure of the leucine aminopeptidase inhibitor microginin FR1., Kraft M, Schleberger C, Weckesser J, Schulz GE, FEBS Lett. 2006 Dec 22;580(30):6943-7. Epub 2006 Dec 4. PMID:17157838

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