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2v5w
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(New page: 200px<br /> <applet load="2v5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v5w, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 20:10, 29 October 2007
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CRYSTAL STRUCTURE OF HDAC8-SUBSTRATE COMPLEX
Overview
Histone deacetylases (HDACs)-an enzyme family that deacetylates histones, and non-histone proteins-are implicated in human diseases such as cancer, and the first-generation of HDAC inhibitors are now in clinical trials., Here, we report the 2.0 A resolution crystal structure of a catalytically, inactive HDAC8 active-site mutant, Tyr306Phe, bound to an acetylated, peptidic substrate. The structure clarifies the role of active-site, residues in the deacetylation reaction and substrate recognition. Notably, the structure shows the unexpected role of a conserved residue at the, active-site rim, Asp 101, in positioning the substrate by directly, interacting with the peptidic backbone and imposing a constrained, cis-conformation. A similar interaction is observed in a new hydroxamate, ... [(full description)]
About this Structure
2V5W is a [Single protein] structure of sequence from [Homo sapiens] with K, ZN, ACE and MCM as [ligands]. Full crystallographic information is available from [OCA].
Reference
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex., Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S, EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:17721440
Page seeded by OCA on Mon Oct 29 22:15:10 2007
Categories: Homo sapiens | Single protein | Carfi, A. | Defrancesco, R. | Gallinari, P. | Jones, P. | Marco, S.Di. | Mattu, M. | Steinkuhler, C. | Vannini, A. | Volpari, C. | ACE | K | MCM | ZN | Alternative splicing | Chromatin | Chromatin regulator | Deacetylation | Hdac | Hdac8 | Histone deacetylase | Hydrolase | Nuclear protein | Nucleus | P53 | Peptidic substrate | Repressor | Transcription | Transcription regulation
