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1okx

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(New page: 200px<br /> <applet load="1okx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1okx, resolution 2.80&Aring;" /> '''BINDING STRUCTURE O...)
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Revision as of 16:21, 29 October 2007

Image:1okx.gif

1okx, resolution 2.80Å

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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]. Active as [[1]], with EC number [3.4.21.36]. 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

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