2b2v

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(New page: 200px<br /> <applet load="2b2v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b2v, resolution 2.65&Aring;" /> '''Crystal structure a...)
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Revision as of 18:51, 12 November 2007


2b2v, resolution 2.65Å

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Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4

Overview

Chromodomains are modules implicated in the recognition of, lysine-methylated histone tails and nucleic acids. CHD (for, chromo-ATPase/helicase-DNA-binding) proteins regulate ATP-dependent, nucleosome assembly and mobilization through their conserved double, chromodomains and SWI2/SNF2 helicase/ATPase domain. The Drosophila CHD1, localizes to the interbands and puffs of the polytene chromosomes, which, are classic sites of transcriptional activity. Other CHD isoforms (CHD3/4, or Mi-2) are important for nucleosome remodelling in histone deacetylase, complexes. Deletion of chromodomains impairs nucleosome binding and, remodelling by CHD proteins. Here we describe the structure of the tandem, arrangement of the human CHD1 chromodomains, and its interactions with, histone tails. Unlike HP1 and Polycomb proteins that use single, chromodomains to bind to their respective methylated histone H3 tails, the, two chromodomains of CHD1 cooperate to interact with one methylated H3, tail. We show that the human CHD1 double chromodomains target the lysine, 4-methylated histone H3 tail (H3K4me), a hallmark of active chromatin., Methylammonium recognition involves two aromatic residues, not the, three-residue aromatic cage used by chromodomains of HP1 and Polycomb, proteins. Furthermore, unique inserts within chromodomain 1 of CHD1 block, the expected site of H3 tail binding seen in HP1 and Polycomb, instead, directing H3 binding to a groove at the inter-chromodomain junction.

About this Structure

2B2V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Double chromodomains cooperate to recognize the methylated histone H3 tail., Flanagan JF, Mi LZ, Chruszcz M, Cymborowski M, Clines KL, Kim Y, Minor W, Rastinejad F, Khorasanizadeh S, Nature. 2005 Dec 22;438(7071):1181-5. PMID:16372014

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