1vkg
From Proteopedia
Crystal Structure of Human HDAC8 complexed with CRA-19156
Overview
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.
About this Structure
1VKG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases., Somoza JR, Skene RJ, Katz BA, Mol C, Ho JD, Jennings AJ, Luong C, Arvai A, Buggy JJ, Chi E, Tang J, Sang BC, Verner E, Wynands R, Leahy EM, Dougan DR, Snell G, Navre M, Knuth MW, Swanson RV, McRee DE, Tari LW, Structure. 2004 Jul;12(7):1325-34. PMID:15242608 Page seeded by OCA on Sat May 3 12:38:34 2008
Categories: Homo sapiens | Single protein | Arvai, A. | Buggy, J J. | Chi, E. | Dougan, D R. | Ho, J D. | Jennings, A J. | Katz, B A. | Knuth, M W. | Leahy, E M. | Luong, C. | McRee, D E. | Mol, C. | Navre, M. | Sang, B C. | Skene, R J. | Snell, G. | Somoza, J R. | Swanson, R V. | Tang, J. | Tari, L W. | Verner, E. | Wynands, R. | Histone deacetylase | Zinc hydrolase
