3D MODELING AND CHARACTERIZATION OF HDAC9
Keywords:
Histone deacetylase, HDAC9, 3D modelling of HDAC9, I-TASSER, RAMPAGE Server, ERRAT ServerAbstract
Objective: Histones are the most abundant proteins associated with the eukaryotic DNA. The N-terminal tails of these histones are subjected to modifications primarily by two enzymes namely, Histone acetyl transferases (HATs) and Histone deacetylases (HDACs). HDACs help in the regulation of the acetylation of histones and the condensation of the chromatin in its sTable form. HDACs are considered as one of the promising targets in cancer biology studies. HDAC9 is a class II member of HDAC family and they are associated with many neurological disorders and a variety of cancers. The 3D structure of this HDAC9(Q9UKV0) was not published. Thus, the aim of this study was to develop and validate the model structure of HDAC9 (Q9UKV0) using bioinformatics tools.
Methods: The Physiochemical characterization was carried out using Ex PASy Prot Param tool, the Functional characterization using Cysteine Recognition Server and HMMTOP Server and Molecular Modeling using I-TASSER. Model Refinement, Validation and verification are carried out using SPDBV, RAMPAGE Server and ERRAT Server respectively.
Result and Conclusion: This3D model of HDAC9 now can be further used to target drug discovery studies related to HDAC9 neurological disorders and a variety of cancers.
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References
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