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赖氨酸特异性去甲基化酶的结构与机制

Structure and mechanism of lysine-specific demethylase enzymes.

作者信息

Anand Ruchi, Marmorstein Ronen

机构信息

Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, Pennsylvania, USA.

出版信息

J Biol Chem. 2007 Dec 7;282(49):35425-9. doi: 10.1074/jbc.R700027200. Epub 2007 Sep 26.

DOI:10.1074/jbc.R700027200
PMID:17897944
Abstract

The discovery of histone-demethylating enzymes has revealed yet another reversible histone modification mark. In this review, we describe the structural and chemical insights that we have now derived underlying the activity of these enzymes. The recent co-crystal structures of LSD1 bound to a proparylamine-derivatized histone H3 peptide and JHDM structures bound to two different methylated histone H3 peptides illustrate the steric requirements and structural basis for substrate specificity.

摘要

组蛋白去甲基化酶的发现揭示了另一种可逆的组蛋白修饰标记。在本综述中,我们描述了目前所获得的有关这些酶活性的结构和化学见解。最近,与丙炔胺衍生化的组蛋白H3肽结合的LSD1共晶体结构以及与两种不同甲基化组蛋白H3肽结合的JHDM结构,阐明了底物特异性的空间要求和结构基础。

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Structure and mechanism of lysine-specific demethylase enzymes.赖氨酸特异性去甲基化酶的结构与机制
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