ArticleThe Journal of biological chemistry2011
Potent family-18 chitinase inhibitors: x-ray structures, affinities, and binding mechanisms.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- DTBind: A Mechanism-Driven Deep Learning Framework for Accurate Prediction of Drug-Target Molecular Recognition.Research (Washington, D.C.) · 2025Article
- Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin intoMarine drugs · 2022Article
- Discovery of Kasugamycin as a Potent Inhibitor of Glycoside Hydrolase Family 18 Chitinases.Frontiers in molecular biosciences · 2021Article
- SyntaLinker: automatic fragment linking with deep conditional transformer neural networks.Chemical science · 2020Article
- Deep Generative Models for 3D Linker Design.Journal of chemical information and modeling · 2020Article
- Structural dissection reveals a general mechanistic principle for group II chitinase (ChtII) inhibition.The Journal of biological chemistry · 2019Article
- Structural Insight Into Chitin Degradation and Thermostability of a Novel Endochitinase From the Glycoside Hydrolase Family 18.Frontiers in microbiology · 2019Article
- Structural characteristics of an insect group I chitinase, an enzyme indispensable to moulting.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Article
- Simplification traps.Journal of chemical biology · 2012Article
- 2-(3,4-Dichloro-phen-yl)-4-phenyl-benzo[h]quinoline.Acta crystallographica. Section E, Structure reports online · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Six novel inhibitors of Vibrio harveyi chitinase A (VhChiA), a family-18 chitinase homolog, were identified by in vitro screening of a library of pharmacologically active compounds. Unlike the previously identified inhibitors that mimicked the reaction intermediates, crystallographic evidence from 14 VhChiA-inhibitor complexes showed that all of the inhibitor molecules occupied the outer part of the substrate-binding cleft at two hydrophobic areas. The interactions at the aglycone location are well defined and tightly associated with Trp-397 and Trp-275, whereas the interactions at the glycone location are patchy, indicating lower affinity and a loose interaction with two consensus residues, Trp-168 and Val-205. When Trp-275 was substituted with glycine (W275G), the binding affinity toward all of the inhibitors dramatically decreased, and in most structures two inhibitor molecules were found to stack against Trp-397 at the aglycone site. Such results indicate that hydrophobic interactions are important for binding of the newly identified inhibitors by the chitinase. X-ray data and isothermal microcalorimetry showed that the inhibitors occupied the active site of VhChiA in three different binding modes, including single-site binding, independent two-site binding, and sequential two-site binding. The inhibitory effect of dequalinium in the low nanomolar range makes this compound an extremely attractive lead compound for plausible development of therapeutics against human diseases involving chitinase-mediated pathologies.
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