Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity
Year: 2018
Type: article
Abstract: Four crystal structures are presented of histone deacetylase 6 (HDAC6) complexes with para -substituted phenylhydromaxamate inhibitors, including bulky peptoids. These structures provide insight regarding the design of capping groups that confer selectivity for binding to HDAC6, specifically with regard to interactions in a pocket formed by the L1 loop. Capping group interactions may also influence hydroxamate-Zn 2+ coordination with monodentate or bidentate geometry.
Source: Journal of Medicinal Chemistry
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Funders: U.S. Department of Energy, Deutsche Forschungsgemeinschaft, National Institutes of Health, Office of Science, National Institute of General Medical Sciences, National Institute of Neurological Disorders and Stroke, Basic Energy Sciences, Biological and Environmental Research, Argonne National Laboratory, SLAC National Accelerator Laboratory
Awards: G102163711, G107546177, G1286251239, G1313983767, G1664757510, G1804828992, G1831385526, G2287611682, G2371548206, G262962599, G2857925935, G3075337988, G324031936, G3479632140, G3488436650, G3629260272, G409777406, G4142084435, G426311843, G4269941704, G4280418065, G498139845, G5036417985, G5387317844, G5607048534, Epigenetic Radiotracers for PET Imaging: Isoform-SelectiveHDAC Probes, G6550344761, G6848031779, G6918803902, G7538797784, G7583137537, G8382000481, A Synchrotron Radiation Structural Biology Resource, NE-CAT Center for Advanced Macromolecular Crystallography, Predoctoral Training at the Chemistry-Biology Interface, Structure and Function of Metalloenzymes, G969889393, G993149817
OpenAlex ID: W2887296525