1t64
From Proteopedia
(New page: 200px<br /> <applet load="1t64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t64, resolution 1.90Å" /> '''Crystal Structure o...) |
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| - | [[Image:1t64. | + | [[Image:1t64.jpg|left|200px]]<br /><applet load="1t64" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1t64, resolution 1.90Å" /> | caption="1t64, resolution 1.90Å" /> | ||
'''Crystal Structure of human HDAC8 complexed with Trichostatin A'''<br /> | '''Crystal Structure of human HDAC8 complexed with Trichostatin A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CA, NA and TSN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=TSN:'>TSN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T64 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc hydrolase]] | [[Category: zinc hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:55:24 2008'' |
Revision as of 14:55, 15 February 2008
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Crystal Structure of human HDAC8 complexed with Trichostatin A
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
1T64 is a Single protein structure of sequence from Homo sapiens with , , and 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 16:55:24 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. | CA | NA | TSN | ZN | Histone deacetylase | Zinc hydrolase
