1eqf: Difference between revisions
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[[Image:1eqf.gif|left|200px]] | [[Image:1eqf.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250''' | {{Structure | ||
|PDB= 1eqf |SIZE=350|CAPTION= <scene name='initialview01'>1eqf</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EQF is a [ | 1EQF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQF OCA]. | ||
==Reference== | ==Reference== | ||
Structure and function of a human TAFII250 double bromodomain module., Jacobson RH, Ladurner AG, King DS, Tjian R, Science. 2000 May 26;288(5470):1422-5. PMID:[http:// | Structure and function of a human TAFII250 double bromodomain module., Jacobson RH, Ladurner AG, King DS, Tjian R, Science. 2000 May 26;288(5470):1422-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10827952 10827952] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
''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 10:59:02 2008'' | ||
Revision as of 11:59, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250
OverviewOverview
TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.
DiseaseDisease
Known diseases associated with this structure: Dystonia-Parkinsonism, X-linked OMIM:[313650]
About this StructureAbout this Structure
1EQF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure and function of a human TAFII250 double bromodomain module., Jacobson RH, Ladurner AG, King DS, Tjian R, Science. 2000 May 26;288(5470):1422-5. PMID:10827952
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