1w22: Difference between revisions

Revision as of 06:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w22.png

Template:STRUCTURE 1w22

CRYSTAL STRUCTURE OF INHIBITED HUMAN HDAC8CRYSTAL STRUCTURE OF INHIBITED HUMAN HDAC8

Template:ABSTRACT PUBMED 15477595

About this StructureAbout this Structure

1W22 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor., Vannini A, Volpari C, Filocamo G, Casavola EC, Brunetti M, Renzoni D, Chakravarty P, Paolini C, De Francesco R, Gallinari P, Steinkuhler C, Di Marco S, Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15064-9. Epub 2004 Oct 11. PMID:15477595

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OCA

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-'''CRYSTAL STRUCTURE OF INHIBITED HUMAN HDAC8'''
+===CRYSTAL STRUCTURE OF INHIBITED HUMAN HDAC8===
-==Overview==
+<!--
-Histone deacetylases (HDACs) are a family of enzymes involved in the regulation of gene expression, DNA repair, and stress response. These processes often are altered in tumors, and HDAC inhibitors have had pronounced antitumor activity with promising results in clinical trials. Here, we report the crystal structure of human HDAC8 in complex with a hydroxamic acid inhibitor. Such a structure of a eukaryotic zinc-dependent HDAC has not be described previously. Similar to bacterial HDAC-like protein, HDAC8 folds in a single alpha/beta domain. The inhibitor and the zinc-binding sites are similar in both proteins. However, significant differences are observed in the length and structure of the loops surrounding the active site, including the presence of two potassium ions in HDAC8 structure, one of which interacts with key catalytic residues. CD data suggest a direct role of potassium in the fold stabilization of HDAC8. Knockdown of HDAC8 by RNA interference inhibits growth of human lung, colon, and cervical cancer cell lines, highlighting the importance of this HDAC subtype for tumor cell proliferation. Our findings open the way for the design and development of selective inhibitors of HDAC8 as possible antitumor agents.
+The line below this paragraph, {{ABSTRACT_PUBMED_15477595}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15477595}}
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 [[Category: Nuclear protein]]
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