Overview

Histone deacetylase 2 (HDAC2) is a key member of the class I histone deacetylase family, which plays a critical role in the epigenetic regulation of gene expression. This enzyme modifies chromatin structure by removing acetyl groups from lysine residues on histone proteins, thereby influencing gene transcription. Although HDAC2 functions in normal cellular processes, it is often overexpressed in various types of cancer and plays a significant role in tumor cell growth, proliferation, and differentiation [1]. As such, HDAC2 is regarded as a promising therapeutic target in cancer treatment.In this study, the binding characteristics of a novel small molecule targeting the HDAC2 enzyme were analyzed in detail. Using computational approaches, molecular docking and molecular dynamics (MD) simulations were conducted to investigate the molecule's binding behavior to the HDAC2 active site. Docking results revealed that the compound binds to the enzyme's active site with high affinity, forming hydrogen bonds and hydrophobic interactions with critical amino acid residues.

Full Product Details

9786209052132

Table of Contents

Reviews

Author Information

Tab Content 6

Countries Available