Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6

Osko, J; Christianson, D.

doi:10.1107/S2053230X20010250

Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6

Journal Article · 01 January 2022 · Acta Crystallographica Section F Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X20010250· OSTI ID:1783946

Osko, J; Christianson, D.

Research Organization:: Brookhaven National Lab. (BNL), Upton, NY (United States)

Sponsoring Organization:: ~OTHER

DOE Contract Number:: SC0012704

OSTI ID:: 1783946

Report Number(s):: BNL-221477-2021-JACI

Journal Information:: Acta Crystallographica Section F Structural Biology Communications, Vol. 76, Issue 9

Country of Publication:: United States

Language:: English

References (53)

Acetylation and Methylation of Histones and Their Possible role in the Regulation of rna Synthesis No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.51.5.786		May 1964
Epigenetic protein families: a new frontier for drug discovery No authors listed Nature Reviews Drug Discovery https://doi.org/10.1038/nrd3674		April 2012
iMOSFLM : a new graphical interface for diffraction-image processing with MOSFLM No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444910048675		March 2011
Discovery of the First-in-Class Dual Histone Deacetylase–Proteasome Inhibitor No authors listed Journal of Medicinal Chemistry https://doi.org/10.1021/acs.jmedchem.8b01487		October 2018
An acetylation–phosphorylation switch that regulates tau aggregation propensity and function No authors listed Journal of Biological Chemistry https://doi.org/10.1074/jbc.M117.794602		September 2017
MolProbity : all-atom structure validation for macromolecular crystallography No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444909042073		December 2009
Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions No authors listed Science https://doi.org/10.1126/science.1175371		July 2009
The acetylation of tau inhibits its function and promotes pathological tau aggregation No authors listed Nature Communications https://doi.org/10.1038/ncomms1255		March 2011
Histone Deacetylase Inhibitors: Overview and Perspectives No authors listed Molecular Cancer Research https://doi.org/10.1158/1541-7786.MCR-07-0324		October 2007
Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL) No authors listed Blood https://doi.org/10.1182/blood-2006-06-025999		September 2006
Features and development of Coot No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444910007493		March 2010
How good are my data and what is the resolution? No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444913000061		June 2013
Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders No authors listed Nature Reviews Drug Discovery https://doi.org/10.1038/nrd4360		August 2014
Three proteins define a class of human histone deacetylases related to yeast Hda1p No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.96.9.4868		April 1999
Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.0430973100		April 2003
Histone deacetylase 6 structure and molecular basis of catalysis and inhibition No authors listed Nature Chemical Biology https://doi.org/10.1038/nchembio.2134		July 2016
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations No authors listed Nucleic Acids Research https://doi.org/10.1093/nar/gku1267		December 2014
HDAC6 is a microtubule-associated deacetylase No authors listed Nature https://doi.org/10.1038/417455a		May 2002
Kinetics and thermodynamics of metal-binding to histone deacetylase 8: Metal-Binding Properties of Histone Deacetylase 8 No authors listed Protein Science https://doi.org/10.1002/pro.2623		January 2015
The unraveling of substrate specificity of histone deacetylase 6 domains using acetylome peptide microarrays and peptide libraries No authors listed The FASEB Journal https://doi.org/10.1096/fj.201801680R		November 2018
Tubulin acetylation: responsible enzymes, biological functions and human diseases No authors listed Cellular and Molecular Life Sciences https://doi.org/10.1007/s00018-015-2000-5		July 2015
Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix No authors listed Acta Crystallographica Section D Structural Biology https://doi.org/10.1107/S2059798319011471		October 2019
Polder maps: improving OMIT maps by excluding bulk solvent No authors listed Acta Crystallographica Section D Structural Biology https://doi.org/10.1107/S2059798316018210		February 2017
Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes No authors listed Current Opinion in Structural Biology https://doi.org/10.1016/j.sbi.2011.08.004		December 2011
Metal-dependent Deacetylases: Cancer and Epigenetic Regulators No authors listed ACS Chemical Biology https://doi.org/10.1021/acschembio.5b01067		February 2016
Multicomponent Synthesis and Binding Mode of Imidazo[1,2- a ]pyridine-Capped Selective HDAC6 Inhibitors No authors listed Organic Letters https://doi.org/10.1021/acs.orglett.8b01118		May 2018
FDA Approval Summary: Vorinostat for Treatment of Advanced Primary Cutaneous T-Cell Lymphoma No authors listed The Oncologist https://doi.org/10.1634/theoncologist.12-10-1247		October 2007
Discovery and development of SAHA as an anticancer agent No authors listed Oncogene https://doi.org/10.1038/sj.onc.1210204		February 2007
Phaser crystallographic software No authors listed Journal of Applied Crystallography https://doi.org/10.1107/S0021889807021206		July 2007
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy No authors listed Neuron https://doi.org/10.1016/j.neuron.2010.08.044		September 2010
Structural insights into HDAC6 tubulin deacetylation and its selective inhibition No authors listed Nature Chemical Biology https://doi.org/10.1038/nchembio.2140		July 2016
HDAC6 inhibition results in tau acetylation and modulates tau phosphorylation and degradation in oligodendrocytes: HDAC6 in Oligodendrocytes No authors listed Glia https://doi.org/10.1002/glia.22624		January 2014
Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6 No authors listed Biochemistry https://doi.org/10.1021/acs.biochem.9b00934		November 2019
Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6 No authors listed Bioorganic & Medicinal Chemistry Letters https://doi.org/10.1016/j.bmcl.2020.127023		April 2020
Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6 No authors listed Journal of Medicinal Chemistry https://doi.org/10.1021/acs.jmedchem.9b01540		December 2019
Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases No authors listed Current Opinion in Structural Biology https://doi.org/10.1016/j.sbi.2019.01.004		December 2019
Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.1718823114		December 2017
Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity No authors listed Journal of Medicinal Chemistry https://doi.org/10.1021/acs.jmedchem.8b01013		April 2018
Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor No authors listed ACS Medicinal Chemistry Letters https://doi.org/10.1021/acsmedchemlett.8b00487		November 2018
Entropy as a Driver of Selectivity for Inhibitor Binding to Histone Deacetylase 6 No authors listed Biochemistry https://doi.org/10.1021/acs.biochem.8b00367		May 2018
Second generation hybrid polar compounds are potent inducers of transformed cell differentiation. No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.93.12.5705		June 1996
Acetylation of intrinsically disordered regions regulates phase separation No authors listed Nature Chemical Biology https://doi.org/10.1038/s41589-018-0180-7		December 2018
Activity-based probes for proteomic profiling of histone deacetylase complexes No authors listed Proceedings of the National Academy of Sciences https://doi.org/10.1073/pnas.0608659104		January 2007
Structural and in Vivo Characterization of Tubastatin A, a Widely Used Histone Deacetylase 6 Inhibitor No authors listed ACS Medicinal Chemistry Letters https://doi.org/10.1021/acsmedchemlett.9b00560		January 2020
The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology No authors listed Cell Reports https://doi.org/10.1016/j.celrep.2017.07.082		August 2017
Identification of a New Family of Higher Eukaryotic Histone Deacetylases: COORDINATE EXPRESSION OF DIFFERENTIATION-DEPENDENT CHROMATIN MODIFIERS No authors listed Journal of Biological Chemistry https://doi.org/10.1074/jbc.274.4.2440		January 1999
50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond No authors listed Nature Reviews Molecular Cell Biology https://doi.org/10.1038/nrm3931		December 2014
New and emerging HDAC inhibitors for cancer treatment No authors listed Journal of Clinical Investigation https://doi.org/10.1172/JCI69738		January 2014
Overview of the CCP 4 suite and current developments No authors listed Acta Crystallographica Section D Biological Crystallography https://doi.org/10.1107/S0907444910045749		March 2011
HDAC6 Deacetylates and Ubiquitinates MSH2 to Maintain Proper Levels of MutSα No authors listed Molecular Cell https://doi.org/10.1016/j.molcel.2014.04.028		July 2014
Two Catalytic Domains Are Required for Protein Deacetylation No authors listed Journal of Biological Chemistry https://doi.org/10.1074/jbc.C500241200		February 2006
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo No authors listed The EMBO Journal https://doi.org/10.1093/emboj/cdg115		March 2003
Characterization of the two catalytic domains in histone deacetylase 6 No authors listed Biochemical and Biophysical Research Communications https://doi.org/10.1016/j.bbrc.2005.12.144		March 2006

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