EC Number   |
|---|
   3.5.1.98 | complex of isoform HDAC9 with myocyte enhancer factor-2 and DNA. HDAC9 binds to a hydrophobic groove of the myocyte enhancer factor-2 dimer. General mechainsm, by which class II histone deacetylases are recruited by myocyte enhancer factor-2 |
| 3.5.1.98 | crystal structure of PA3774 from Pseudomonas aeruginosa as ligand-free enzyme and as protein-ligand complexes with a trifluoromethylketone inhibitor and the reaction product acetate, and of inhibitor-free PA3774H143A mutant, the inhibitor-free PA3774Y313F mutant, and the PA3774Y313F mutant in complex with the highly selective hydroxamate inhibitor N-[1,1,2,2,3,3,4,4,5,5,6,6-dodecafluoro-7-(hydroxyamino)-7-oxoheptyl]benzamide, from 0.5 M K2HPO4, 0.5 M Na2HPO4, and 0.1 M (NH4)2SO4, pH 7.5, X-ray diffraction structure determination and analysis |
| 3.5.1.98 | docking studies of the representative compound 4 to the homology model of HDAC1 and the X-ray structures of HDAH, PDB 1ZZ1, and HDAC8, PDB 1T67 |
| 3.5.1.98 | free enzyme and in complexes with inhibitors trichostatin A and suberoylanilide hydroxamic acid. Active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems |
| 3.5.1.98 | Hda1 ARB2 domain, native and selenomethionine-labebeed protein, hanging drop vapour diffusion method, from 0.1 M sodium acetate trihydrate, pH 4.6, and 2.0 M sodium formate, 12°C, 1 day, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement method and modelling |
| 3.5.1.98 | modeling studies using inhibitor 6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide and histone deacetylase-like protein, PDB ID: 1C3R. Inhibitor fills the equivalent space at the protein surface and occupies the catalytic binding site, coordinating the fundamental zinc ion |
| 3.5.1.98 | molecular modeling of isoform HDAC8 in complex with inhibitor N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide |
| 3.5.1.98 | molecular modelling of structure of isoform HDAC8 in complex with suberoylanilide hydroxamic acid and with 7-mercapto-N-phenylheptanamide |
| 3.5.1.98 | N-terminal glutamine-rich fragment, residues 62-153. The glutamine-rich domain folds into an alpha-helix that assembles as a tetramer lacking regularly arranged apolar residues and an extended hydrophobic core. Instead, the protein interfaces consist of multiple hydrophobic patches interspersed with polar interaction networks, wherein clusters of glutamines engage in extensive intra- and interhelical interactions. In solution, the tetramer undergoes rapid equilibrium with monomer and intermediate species |
| 3.5.1.98 | seven structures of wild-type HDAC8 and mutants in complex with inhibitors or substrate are determined to a resolution of 1.8 to 3.3 A |
