1t67: Difference between revisions

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[[Image:1t67.~~jpg~~|left|200px]]

[[Image:1t67.png|left|200px]]

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~~'''~~Crystal Structure of Human HDAC8 complexed with MS-344~~'''~~

===Crystal Structure of Human HDAC8 complexed with MS-344===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_15242608}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15242608 is the PubMed ID number.

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==About this Structure==

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[[Category: Histone deacetylase]]

[[Category: Zinc hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 09~~:34:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:54:42 2008''

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-[[Image:1t67.jpg|left|200px]]
+{{Seed}}
+[[Image:1t67.png|left|200px]]
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 {{STRUCTURE_1t67|  PDB=1t67  |  SCENE=  }}
-'''Crystal Structure of Human HDAC8 complexed with MS-344'''
+===Crystal Structure of Human HDAC8 complexed with MS-344===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15242608}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15242608 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15242608}}
 ==About this Structure==
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 [[Category: Histone deacetylase]]
 [[Category: Zinc hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:34:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:54:42 2008''