1n72: Difference between revisions
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[[Image:1n72.gif|left|200px]] | [[Image:1n72.gif|left|200px]] | ||
'''Structure and Ligand of a Histone Acetyltransferase Bromodomain''' | {{Structure | ||
|PDB= 1n72 |SIZE=350|CAPTION= <scene name='initialview01'>1n72</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= PCAF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structure and Ligand of a Histone Acetyltransferase Bromodomain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1N72 is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10365964 10365964] | ||
[[Category: Histone acetyltransferase]] | [[Category: Histone acetyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: histone acetyltransferase bromodomain]] | [[Category: histone acetyltransferase bromodomain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:00 2008'' | ||
Revision as of 13:53, 20 March 2008
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| Gene: | PCAF (Homo sapiens) | ||||||
| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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