1eqf
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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 SO4 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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