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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-10-21
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pubmed:abstractText |
Interferon regulatory factor 1 (IRF-1) is an essential factor involved in the regulation of type I interferon (IFN) and IFN-inducible genes. The protein consists of 329 amino acids that are highly conserved from mouse to human. Similar to other transcription factors, the protein is modular in nature with a basic N-terminal region involved in DNA binding and an acidic C-terminal region required for activation. We report here the expression, purification and co-crystallization of the minimal N-terminal region of IRF-1 involved in DNA binding (amino acids 1-113) with a 13 bp DNA fragment from the IFN-beta promoter. The crystals diffract to at least 3.0 A in resolution and belong to space group R3 with unit cell parameters of a = b = 84.8 A, c = 203.7 A.
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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 |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
414
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-20
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9315689-Base Sequence,
pubmed-meshheading:9315689-Binding Sites,
pubmed-meshheading:9315689-Cloning, Molecular,
pubmed-meshheading:9315689-Crystallography, X-Ray,
pubmed-meshheading:9315689-DNA-Binding Proteins,
pubmed-meshheading:9315689-Escherichia coli,
pubmed-meshheading:9315689-Interferon Regulatory Factor-1,
pubmed-meshheading:9315689-Interferon-beta,
pubmed-meshheading:9315689-Oligodeoxyribonucleotides,
pubmed-meshheading:9315689-Papain,
pubmed-meshheading:9315689-Peptide Fragments,
pubmed-meshheading:9315689-Phosphoproteins,
pubmed-meshheading:9315689-Promoter Regions, Genetic,
pubmed-meshheading:9315689-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
Expression, purification, and co-crystallization of IRF-I bound to the interferon-beta element PRDI.
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pubmed:affiliation |
Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA.
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pubmed:publicationType |
Journal Article
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