1n72: Difference between revisions

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[[Image:1n72.gif|left|200px]]
[[Image:1n72.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1n72", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span>
or leave the SCENE parameter empty for the default display.
|GENE= PCAF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n72 OCA], [http://www.ebi.ac.uk/pdbsum/1n72 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n72 RCSB]</span>
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'''Structure and Ligand of a Histone Acetyltransferase Bromodomain'''
'''Structure and Ligand of a Histone Acetyltransferase Bromodomain'''
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==About this Structure==
==About this Structure==
1N72 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1B91. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N72 OCA].  
1N72 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b91 1b91]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N72 OCA].  


==Reference==
==Reference==
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[[Category: Zhou, M M.]]
[[Category: Zhou, M M.]]
[[Category: 4-helical bundle]]
[[Category: 4-helical bundle]]
[[Category: histone acetyltransferase bromodomain]]
[[Category: Histone acetyltransferase bromodomain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:10:37 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:16 2008''

Revision as of 02:10, 3 May 2008

File:1n72.gif

Template:STRUCTURE 1n72

Structure and Ligand of a Histone Acetyltransferase Bromodomain


OverviewOverview

Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.

About this StructureAbout this Structure

1N72 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1b91. Full crystallographic information is available from OCA.

ReferenceReference

Structure and ligand of a histone acetyltransferase bromodomain., Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM, Nature. 1999 Jun 3;399(6735):491-6. PMID:10365964 Page seeded by OCA on Sat May 3 02:10:37 2008

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