1eqf: Difference between revisions

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New page: left|200px<br /> <applet load="1eqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqf, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1eqf.gif|left|200px]]<br />
[[Image:1eqf.gif|left|200px]]<br /><applet load="1eqf" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1eqf" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1eqf, resolution 2.1&Aring;" />
caption="1eqf, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250'''<br />
'''CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250'''<br />


==Overview==
==Overview==
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.
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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1EQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQF OCA].  
1EQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQF OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Jacobson, R.H.]]
[[Category: Jacobson, R H.]]
[[Category: King, D.S.]]
[[Category: King, D S.]]
[[Category: Ladurner, A.G.]]
[[Category: Ladurner, A G.]]
[[Category: Tjian, R.]]
[[Category: Tjian, R.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: four-helix bundle]]
[[Category: four-helix bundle]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:45:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:29 2008''

Revision as of 13:30, 21 February 2008

File:1eqf.gif


1eqf, resolution 2.1Å

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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 with as ligand. 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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