1w22

From Proteopedia

Revision as of 11:29, 30 October 2007

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 ... [(full description)]

About this Structure

1W22 is a [Single protein] structure of sequence from [Homo sapiens] with ZN, K and NHB as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

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

Page seeded by OCA on Tue Oct 30 13:34:36 2007