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rdf:type |
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lifeskim:mentions |
umls-concept:C0024485,
umls-concept:C0040649,
umls-concept:C0080347,
umls-concept:C0205112,
umls-concept:C0205314,
umls-concept:C0337076,
umls-concept:C0450363,
umls-concept:C0679622,
umls-concept:C1136073,
umls-concept:C1148672,
umls-concept:C1420622,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2603343
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pubmed:issue |
38
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pubmed:dateCreated |
1993-11-2
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pubmed:abstractText |
Transcriptional elongation provides a key control point in the regulation of eukaryotic gene expression. Here we describe homonuclear and 15N-heteronuclear 3D NMR studies of the nucleic acid binding domain of human transcriptional elongation factor TFIIS. This domain contains a Cys4 Zn(2+)-binding site with no homology to previously characterized Cys4, Cys6, or Cys2-His2 Zn fingers. Complete 1H and 15N NMR resonance assignment of a 50-residue TFIIS peptide-Zn2+ complex is obtained. Its solution structure, as determined by distance geometry/simulated annealing (DG/SA) calculations, exhibits a novel three-stranded antiparallel beta-sheet (designated the Zn ribbon). Analogous sequence motifs occur in a wide class of proteins involved in RNA or DNA transactions, including human basal transcriptional initiation factor TFIIE. A three-dimensional model of the TFIIE Cys4 domain is obtained by DG-based homology modeling. The role of the TFIIS Zn ribbon in the control of eukaryotic transcriptional elongation is discussed.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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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 |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9944-59
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8399164-Amino Acid Sequence,
pubmed-meshheading:8399164-Animals,
pubmed-meshheading:8399164-Binding Sites,
pubmed-meshheading:8399164-Cloning, Molecular,
pubmed-meshheading:8399164-Escherichia coli,
pubmed-meshheading:8399164-Humans,
pubmed-meshheading:8399164-Hydrogen Bonding,
pubmed-meshheading:8399164-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8399164-Models, Molecular,
pubmed-meshheading:8399164-Models, Structural,
pubmed-meshheading:8399164-Molecular Sequence Data,
pubmed-meshheading:8399164-Neoplasm Proteins,
pubmed-meshheading:8399164-Protein Folding,
pubmed-meshheading:8399164-Protein Structure, Secondary,
pubmed-meshheading:8399164-Recombinant Proteins,
pubmed-meshheading:8399164-Sequence Homology, Amino Acid,
pubmed-meshheading:8399164-Transcription, Genetic,
pubmed-meshheading:8399164-Transcription Factors,
pubmed-meshheading:8399164-Transcription Factors, General,
pubmed-meshheading:8399164-Transcriptional Elongation Factors,
pubmed-meshheading:8399164-Zinc Fingers
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pubmed:year |
1993
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pubmed:articleTitle |
Novel zinc finger motif in the basal transcriptional machinery: three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS.
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pubmed:affiliation |
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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