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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6572
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pubmed:dateCreated |
1996-4-22
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pubmed:abstractText |
A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Box Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Taf6 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/e(y)1 protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
380
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
316-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8598927-Amino Acid Sequence,
pubmed-meshheading:8598927-Animals,
pubmed-meshheading:8598927-Chickens,
pubmed-meshheading:8598927-Crystallography, X-Ray,
pubmed-meshheading:8598927-DNA-Binding Proteins,
pubmed-meshheading:8598927-Drosophila,
pubmed-meshheading:8598927-Drosophila Proteins,
pubmed-meshheading:8598927-Escherichia coli,
pubmed-meshheading:8598927-Histones,
pubmed-meshheading:8598927-Models, Molecular,
pubmed-meshheading:8598927-Molecular Sequence Data,
pubmed-meshheading:8598927-Protein Conformation,
pubmed-meshheading:8598927-RNA Polymerase II,
pubmed-meshheading:8598927-Recombinant Proteins,
pubmed-meshheading:8598927-Sequence Alignment,
pubmed-meshheading:8598927-TATA-Binding Protein Associated Factors,
pubmed-meshheading:8598927-TATA-Box Binding Protein,
pubmed-meshheading:8598927-Trans-Activators,
pubmed-meshheading:8598927-Transcription Factor TFIID,
pubmed-meshheading:8598927-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
Structural similarity between TAFs and the heterotetrameric core of the histone octamer.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, The Rockefeller University, New York, 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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