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| - | [[Image:2b2v.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2b2v| PDB=2b2v | SCENE= }} | | {{STRUCTURE_2b2v| PDB=2b2v | SCENE= }} |
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| - | '''Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4'''
| + | ===Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16372014}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16372014 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16372014}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Monomethyllysine]] | | [[Category: Monomethyllysine]] |
| | [[Category: Three stranded antiparallel beta sheet]] | | [[Category: Three stranded antiparallel beta sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:46:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:24:25 2008'' |
Revision as of 14:24, 27 July 2008
Template:STRUCTURE 2b2v
Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4
Template:ABSTRACT PUBMED 16372014
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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