1t69
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1t69.gif|left|200px]] | + | [[Image:1t69.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of human HDAC8 complexed with SAHA''' | + | {{Structure |
+ | |PDB= 1t69 |SIZE=350|CAPTION= <scene name='initialview01'>1t69</scene>, resolution 2.91Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SHH:OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE'>SHH</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of human HDAC8 complexed with SAHA''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1T69 is a [ | + | 1T69 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T69 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15242608 15242608] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 40: | Line 49: | ||
[[Category: zinc hydrolase]] | [[Category: zinc hydrolase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:21 2008'' |
Revision as of 12:14, 20 March 2008
| |||||||
, resolution 2.91Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of human HDAC8 complexed with SAHA
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
1T69 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 Thu Mar 20 14:14:21 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. | SHH | ZN | Histone deacetylase | Zinc hydrolase