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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2006-6-7
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pubmed:abstractText |
Histone deacetylases (HDACs) are key enzymes in the transcriptional regulation of gene expression in eukaryotic cells. In recent years HDACs 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 1 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0168-1656
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pubmed:author |
pubmed-author:FicnerRalfR,
pubmed-author:GiuratoLauraL,
pubmed-author:GuccioneSalvatoreS,
pubmed-author:HempelRenéR,
pubmed-author:HildmannChristianC,
pubmed-author:MeranaJoachimJ,
pubmed-author:NielsenTine KraghTK,
pubmed-author:RiesterDanielD,
pubmed-author:SchoberAndreasA,
pubmed-author:SchwienhorstAndreasA,
pubmed-author:WegenerDennisD
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
124
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
258-70
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16567013-Amino Acid Sequence,
pubmed-meshheading:16567013-Amino Acid Substitution,
pubmed-meshheading:16567013-Binding Sites,
pubmed-meshheading:16567013-Crystallography, X-Ray,
pubmed-meshheading:16567013-Histone Deacetylase Inhibitors,
pubmed-meshheading:16567013-Histone Deacetylases,
pubmed-meshheading:16567013-Humans,
pubmed-meshheading:16567013-Hydrogen-Ion Concentration,
pubmed-meshheading:16567013-Hydroxamic Acids,
pubmed-meshheading:16567013-Inhibitory Concentration 50,
pubmed-meshheading:16567013-Kinetics,
pubmed-meshheading:16567013-Models, Molecular,
pubmed-meshheading:16567013-Molecular Structure,
pubmed-meshheading:16567013-Protein Binding,
pubmed-meshheading:16567013-Protein Structure, Secondary,
pubmed-meshheading:16567013-Repressor Proteins,
pubmed-meshheading:16567013-Structure-Activity Relationship,
pubmed-meshheading:16567013-Substrate Specificity
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pubmed:year |
2006
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pubmed:articleTitle |
Substrate and inhibitor specificity of class 1 and class 2 histone deacetylases.
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pubmed:affiliation |
Department of Molecular Genetics and Preparative Molecular Biology Institute for Microbiology und Genetics, Goettingen, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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