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1h0g

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[[Category: inhibitor]]
[[Category: inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:53:46 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:24:37 2007''

Revision as of 13:19, 30 October 2007

Image:1h0g.gif

1h0g, resolution 2.00Å

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COMPLEX OF A CHITINASE WITH THE NATURAL PRODUCT CYCLOPENTAPEPTIDE ARGADIN FROM CLONOSTACHYS

Overview

Over the past years, family 18 chitinases have been validated as potential, targets for the design of drugs against human pathogens that contain or, interact with chitin during their normal life cycles. Thus far, only one, potent chitinase inhibitor has been described in detail, the, pseudotrisaccharide allosamidin. Recently, however, two potent, natural-product cyclopentapeptide chitinase inhibitors, argifin and, argadin, were reported. Here, we describe high-resolution crystal, structures that reveal the details of the interactions of these, cyclopeptides with a family 18 chitinase. The structures are examples of, complexes of a carbohydrate-processing enzyme with high-affinity, peptide-based inhibitors and show in detail how the peptide backbone and, side chains mimic the interactions ... [(full description)]

About this Structure

1H0G is a [Protein complex] structure of sequences from [Serratia marcescens] with ACE and GOL as [ligands]. Active as [Hydrolase], with EC number [3.2.1.14.]. Structure known Active Site: GB1. Full crystallographic information is available from [OCA].

Reference

High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate., Houston DR, Shiomi K, Arai N, Omura S, Peter MG, Turberg A, Synstad B, Eijsink VG, van Aalten DM, Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9127-32. Epub 2002 Jul 1. PMID:12093900

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