Journal
JOURNAL OF BIOTECHNOLOGY
Volume 124, Issue 1, Pages 258-270Publisher
ELSEVIER
DOI: 10.1016/j.jbiotec.2006.01.030
Keywords
histone deacetylase; FB188HDAH; substrate specificity; hydroxamate inhibitors; X-ray crystallographic structure; cancer therapy
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Histone deacetylases (HDACs) are key enzymes in the transcriptional regulation of gene expression in eukaryotic cells. In recent years MACs have attracted considerable attention as promising new targets in anticancer therapy. Currently, different histone deacetylase subtypes are divided into four groups denoted as classes 1-4. Here, we compare in more detail representatives of class I HDACs and FB188 HDAH as a close bacterial homologue of class 2 HDAC6, in regard of substrate and inhibitor specificity. Structure comparison is used to identify candidate regions responsible for observed specificity differences. Knowledge of these structural elements expedite studies on the biochemical role of different HDAC subtypes as well as the development of highly selective HDAC inhibitors as antitumor agents. (c) 2006 Elsevier B.V. All rights reserved.
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