1t67 | pdb_00001t67
Crystal Structure of Human HDAC8 complexed with MS-344
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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
1T67 is a Single protein structure of sequence from Homo sapiens with ZN, NA and B3N as ligands. 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 Fri Feb 15 16:55:27 2008
Proteopedia Page Contributors and Editors (what is this?)
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- 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.
- B3N
- NA
- ZN
- Histone deacetylase
- Zinc hydrolase
