3SFF

Crystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived Inhibitor

Summary for 3SFF

• Entry DOI: 10.2210/pdb3sff/pdb
• Related: 3SFH
• Descriptor: Histone deacetylase 8, (2R)-2-amino-3-(3-chlorophenyl)-1-[4-(2,5-difluorobenzoyl)piperazin-1-yl]propan-1-one, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: deacetylase, nvp-lci785, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9BY41
• Total number of polymer chains: 1
• Total formula weight: 42441.00

Authors

Stams, T.,Vash, B. (deposition date: 2011-06-13, release date: 2011-07-20, Last modification date: 2024-02-28)

Primary citation

Whitehead, L.,Dobler, M.R.,Radetich, B.,Zhu, Y.,Atadja, P.W.,Claiborne, T.,Grob, J.E.,McRiner, A.,Pancost, M.R.,Patnaik, A.,Shao, W.,Shultz, M.,Tichkule, R.,Tommasi, R.A.,Vash, B.,Wang, P.,Stams, T.
Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors.
Bioorg.Med.Chem., 19:4626-4634, 2011

PubMed Abstract: Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X-ray crystallography and molecular modeling of these novel inhibitors bound to HDAC8, potentially revealing insights into the mechanism of enzymatic function through novel structural features revealed at the atomic level.

PubMed: 21723733
DOI: 10.1016/j.bmc.2011.06.030

Experimental method

X-RAY DIFFRACTION (2 Å)