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rdf:type |
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lifeskim:mentions |
umls-concept:C0003765,
umls-concept:C0012854,
umls-concept:C0026336,
umls-concept:C0037633,
umls-concept:C0439855,
umls-concept:C0678594,
umls-concept:C1336789,
umls-concept:C1382100,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
10
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pubmed:dateCreated |
1997-11-13
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pubmed:abstractText |
The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.
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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/ArgR protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/ArgR protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
819-26
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9334747-Amino Acid Sequence,
pubmed-meshheading:9334747-Bacterial Proteins,
pubmed-meshheading:9334747-Base Sequence,
pubmed-meshheading:9334747-Binding Sites,
pubmed-meshheading:9334747-Cloning, Molecular,
pubmed-meshheading:9334747-DNA,
pubmed-meshheading:9334747-DNA-Binding Proteins,
pubmed-meshheading:9334747-Escherichia coli Proteins,
pubmed-meshheading:9334747-Helix-Turn-Helix Motifs,
pubmed-meshheading:9334747-Macromolecular Substances,
pubmed-meshheading:9334747-Models, Molecular,
pubmed-meshheading:9334747-Molecular Sequence Data,
pubmed-meshheading:9334747-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9334747-Nucleic Acid Conformation,
pubmed-meshheading:9334747-Protein Structure, Secondary,
pubmed-meshheading:9334747-Recombinant Proteins,
pubmed-meshheading:9334747-Repressor Proteins,
pubmed-meshheading:9334747-Solutions
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pubmed:year |
1997
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pubmed:articleTitle |
Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA.
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pubmed:affiliation |
Karolinska Institute, Department of Medical Biochemistry and Biophysics, Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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