Structural highlights
2j9a is a 2 chain structure with sequence from Bos taurus and Microcystis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| NonStd Res: | |
| Related: | 1bll, 1bpm, 1bpn, 1lam, 1lan, 1lap, 1lcp, 2ewb |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[AMPL_BOVIN] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kraft M, Schleberger C, Weckesser J, Schulz GE. Binding structure of the leucine aminopeptidase inhibitor microginin FR1. FEBS Lett. 2006 Dec 22;580(30):6943-7. Epub 2006 Dec 4. PMID:17157838 doi:10.1016/j.febslet.2006.11.060
