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1T69

Crystal Structure of human HDAC8 complexed with SAHA

Summary for 1T69
Entry DOI10.2210/pdb1t69/pdb
Related1T64 1T67
DescriptorHistone deacetylase 8, ZINC ION, OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE (3 entities in total)
Functional Keywordshistone deacetylase, zinc hydrolase, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q9BY41
Total number of polymer chains1
Total formula weight42132.21
Authors
Primary citationSomoza, J.R.,Skene, R.J.,Katz, B.A.,Mol, C.,Ho, J.D.,Jennings, A.J.,Luong, C.,Arvai, A.,Buggy, J.J.,Chi, E.,Tang, J.,Sang, B.-C.,Verner, E.,Wynands, R.,Leahy, E.M.,Dougan, D.R.,Snell, G.,Navre, M.,Knuth, M.W.,Swanson, R.V.,McRee, D.E.,Tari, L.W.
Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases
Structure, 12:1325-1334, 2004
Cited by
PubMed Abstract: Modulation of the acetylation state of histones plays a pivotal role in the regulation of gene expression. Histone deacetylases (HDACs) catalyze the removal of acetyl groups from lysines near the N termini of histones. This reaction promotes the condensation of chromatin, leading to repression of transcription. HDAC deregulation has been linked to several types of cancer, suggesting a potential use for HDAC inhibitors in oncology. Here we describe the first crystal structures of a human HDAC: the structures of human HDAC8 complexed with four structurally diverse hydroxamate inhibitors. This work sheds light on the catalytic mechanism of the HDACs, and on differences in substrate specificity across the HDAC family. The structure also suggests how phosphorylation of Ser39 affects HDAC8 activity.
PubMed: 15242608
DOI: 10.1016/j.str.2004.04.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.91 Å)
Structure validation

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数据于2024-10-30公开中

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