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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Investigating Potential Cancer Therapeutics: Insight into Histone Deacetylases (HDACs) Inhibitions.

Basharat Ahmad1, Aamir Saeed2, Ahmed Al-Amery3

  • 1School of Life Science and Technology, Center for Informational Biology, University of Electronics Science and Technology of China, Chengdu 610056, China.

Pharmaceuticals (Basel, Switzerland)
|April 27, 2024
PubMed
Summary

Researchers identified novel inhibitors, LIG1 and LIG2, targeting histone deacetylases (HDACs) for cancer therapy. Molecular docking and simulations revealed their potential to disrupt cancer-linked HDAC enzyme activity and protein structure.

Keywords:
histone deacetylasesmolecular dockingmolecular dynamic simulationneuroblastoma

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Area of Science:

  • Medicinal Chemistry
  • Computational Biology
  • Biochemistry

Background:

  • Histone deacetylases (HDACs) are crucial enzymes involved in cancer development.
  • Targeting HDACs offers a promising therapeutic strategy for various cancers.

Purpose of the Study:

  • To discover novel, selective inhibitors for cancer-associated HDAC enzymes.
  • To investigate the molecular mechanisms of potential HDAC inhibitors.

Main Methods:

  • Molecular docking using MOE to screen ZINC database compounds against HDACs.
  • Molecular dynamics (MD) simulations to analyze binding affinities and protein-ligand interactions.
  • Analysis of protein flexibility using RMSD, RMSF, Rg, and Principal Component Analysis (PCA).

Main Results:

  • Two stable inhibitors, LIG1 and LIG2, were identified with favorable binding.
  • MD simulations showed LIG1 and LIG2 impact HDAC flexibility and induce structural changes.
  • PCA analysis indicated that inhibitor activity alters HDAC structural dynamics.

Conclusions:

  • LIG1 and LIG2 demonstrate potential as effective HDAC inhibitors.
  • The study provides a basis for further investigation of these compounds in cancer treatment.
  • Understanding inhibitor-induced structural dynamics is key for drug design.