2a3e

Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin

spinqualitylabelsall models 2a3e, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2a3e is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMI, SO4, NAA Related: 1w9p, 1w9v, 1w9u, 1hkk, 2a3a, 2a3b, 2a3c Activity: Chitinase, with EC number 3.2.1.14 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 Family 18 chitinases play key roles in a range of pathogenic organisms and are overexpressed in the asthmatic lung. By screening a library of marketed drug molecules, we have identified methylxanthine derivatives as possible inhibitor leads. These derivatives, theophylline, caffeine, and pentoxifylline, are used therapeutically as antiinflammatory agents, with pleiotropic mechanisms of action. Here it is shown that they are also competitive inhibitors against a fungal family 18 chitinase, with pentoxifylline being the most potent (K(i) of 37 microM). Crystallographic analysis of chitinase-inhibitor complexes revealed specific interactions with the active site, mimicking the reaction intermediate analog, allosamidin. Mutagenesis identified the key active site residues, conserved in mammalian chitinases, which contribute to inhibitor affinity. Enzyme assays also revealed that these methylxanthines are active against human chitinases. Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes.,Rao FV, Andersen OA, Vora KA, Demartino JA, van Aalten DM Chem Biol. 2005 Sep;12(9):973-80. PMID:16183021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase

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