1w9p
SPECIFICITY AND AFFINITY OF NATURAL PRODUCT CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRA
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OverviewOverview
Family 18 chitinases play key roles in organisms ranging from bacteria to, man. There is a need for specific, potent inhibitors to probe the function, of these chitinases in different organisms. Such molecules could also, provide leads for the development of chemotherapeuticals with fungicidal, insecticidal, or anti-inflammatory potential. Recently, two natural, product peptides, argifin and argadin, have been characterized, which, structurally mimic chitinase-chitooligosaccharide interactions and inhibit, a bacterial chitinase in the nM-mM range. Here, we show that these, inhibitors also act on human and Aspergillus fumigatus chitinases. The, structures of these enzymes in complex with argifin and argadin, together, with mutagenesis, fluorescence, and enzymology, reveal that subtle ... [(full description)]
About this StructureAbout this Structure
1W9P is a [Single protein] structure of sequence from [Aspergillus fumigatus] with SO4 as [ligand]. Active as [Chitinase], with EC number [3.2.1.14]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases., Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, Shiomi K, Omura S, van Aalten DM, Chem Biol. 2005 Jan;12(1):65-76. PMID:15664516
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