From Proteopedia

Revision as of 19:27, 7 April 2019

Histone Deacetylase 8 (HDAC 8)

Introduction

Histone deacetylase 8 (HDAC 8) is an enzyme that plays a role in controlling gene expression. Specifically, it catalyzes the removal of an acetyl group off of the ε-amino-lysine sidechain of N-terminal core of Histone proteins. By removing the acetate ion, the reclaimed positive charge on the lysine sidechain is able to interact with the negative charge on the DNA. As a result, DNA will bind more tightly to the histone protein reducing transcription and expression.

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Homology 1.1 Classes 1.2 Sequence Alignment 2 Structural Highlights 2.1 Zinc Ion 2.2 Key Residues 2.3 Binding Pocket 3 Mechanism 4 Relevance 4.1 Gene Expression 4.2 Disease 4.3 HDAC Inhibitors Homology Classes Sequence Alignment Structural Highlights Zinc Ion Key Residues Binding Pocket Mechanism Similar to many serine and zinc proteases, HDAC8 uses a mechanism with a "catalytic triad." Instead of the Asp-His-Ser, HDAC8 uses the His to coordinate a H2O nucleophile. Relevance Gene Expression Disease HDAC Inhibitors This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

1. Whitehead, L., Dobler, M. R., Radetich, B., Zhu, Y., Atadja, P. W., Claiborne, T., ... & Shao, W. (2011). Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors. Bioorganic & medicinal chemistry, 19(15), 4626-4634.