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1okx
From Proteopedia
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| , resolution 2.80Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BINDING STRUCTURE OF ELASTASE INHIBITOR SCYPTOLIN A
Overview
Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.8 A resolution. The inhibitor occupies the most prominent subsites S1 through S4 of the elastase and prevents a hydrolytic attack by covering the active center with its rigid ring structure. The observed binding structure may help to design potent elastase inhibitors.
About this Structure
1OKX is a Protein complex structure of sequences from Scytonema hofmanni and Sus scrofa. Full crystallographic information is available from OCA.
Reference
Binding structure of elastase inhibitor scyptolin A., Matern U, Schleberger C, Jelakovic S, Weckesser J, Schulz GE, Chem Biol. 2003 Oct;10(10):997-1001. PMID:14583266
Page seeded by OCA on Sun Mar 30 22:46:48 2008
