1n72
From Proteopedia
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[[Image:1n72.gif|left|200px]] | [[Image:1n72.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1n72| PDB=1n72 | SCENE= }} | |
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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 | + | 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: | + | [[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 | + | |
Revision as of 23:10, 2 May 2008
Structure and Ligand of a Histone Acetyltransferase Bromodomain
Overview
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 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.
Reference
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
