1c3s: Difference between revisions

Revision as of 20:10, 30 June 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:1c3s.png

Template:STRUCTURE 1c3s

CRYSTAL STRUCTURE OF AN HDAC HOMOLOG COMPLEXED WITH SAHACRYSTAL STRUCTURE OF AN HDAC HOMOLOG COMPLEXED WITH SAHA

Template:ABSTRACT PUBMED 10490031

About this StructureAbout this Structure

1C3S is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors., Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, Breslow R, Pavletich NP, Nature. 1999 Sep 9;401(6749):188-93. PMID:10490031

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF AN HDAC HOMOLOG COMPLEXED WITH SAHA'''
+===CRYSTAL STRUCTURE OF AN HDAC HOMOLOG COMPLEXED WITH SAHA===
-==Overview==
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-Histone deacetylases (HDACs) mediate changes in nucleosome conformation and are important in the regulation of gene expression. HDACs are involved in cell-cycle progression and differentiation, and their deregulation is associated with several cancers. HDAC inhibitors, such as trichostatin A (TSA) and suberoylanilide hydroxamic acid (SAHA), have anti-tumour effects, as they can inhibit cell growth, induce terminal differentiation and prevent the formation of tumours in mice models, and they are effective in the treatment of promyelocytic leukemia. Here we describe the structure of the histone deacetylase catalytic core, as revealed by the crystal structure of a homologue from the hyperthermophilic bacterium Aquifex aeolicus, that shares 35.2% identity with human HDAC1 over 375 residues, deacetylates histones in vitro and is inhibited by TSA and SAHA. The deacetylase, deacetylase-TSA and deacetylase-SAHA structures reveal an active site consisting of a tubular pocket, a zinc-binding site and two Asp-His charge-relay systems, and establish the mechanism of HDAC inhibition. The residues that make up the active site and contact the inhibitors are conserved across the HDAC family. These structures also suggest a mechanism for the deacetylation reaction and provide a framework for the further development of HDAC inhibitors as antitumour agents.
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 ==About this Structure==
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 [[Category: Hydroxamic acid]]
 [[Category: Penta-coordinated zinc]]
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