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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 |
2001-1-10
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pubmed:abstractText |
A 12 bp long GCN4-binding, self-complementary duplex DNA d(CATGACGTCATG)(2) has been investigated by NMR spectroscopy to study the structure and dynamics of the molecule in aqueous solution. The NMR structure of the DNA obtained using simulated annealing and iterative relaxation matrix calculations compares quite closely with the X-ray structure of ATF/CREB DNA in complex with GCN4 protein (DNA-binding domain). The DNA is also seen to be curved in the free state and this has a significant bearing on recognition by the protein. The dynamic characteristics of the molecule have been studied by (13)C relaxation measurements at natural abundance. A correlation has been observed between sequence-dependent dynamics and recognition by GCN4 protein.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-1328653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-1473154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-1723809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-2145515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-2204954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-2482765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-2690953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-6387704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-6433345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-6547529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-7500340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-7514039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-7531772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-7830599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-7881272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-8178171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-8219742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-8458331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-8953216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11139620-9548924
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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 |
Jan
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-505
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11139620-Crystallography, X-Ray,
pubmed-meshheading:11139620-DNA,
pubmed-meshheading:11139620-DNA-Binding Proteins,
pubmed-meshheading:11139620-Fungal Proteins,
pubmed-meshheading:11139620-Models, Molecular,
pubmed-meshheading:11139620-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11139620-Nucleoside Diphosphate Sugars,
pubmed-meshheading:11139620-Protein Kinases,
pubmed-meshheading:11139620-Protein Structure, Quaternary,
pubmed-meshheading:11139620-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11139620-Solubility,
pubmed-meshheading:11139620-Substrate Specificity,
pubmed-meshheading:11139620-Thermodynamics
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pubmed:year |
2001
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pubmed:articleTitle |
Solution structure and dynamics of GCN4 cognate DNA: NMR investigations.
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pubmed:affiliation |
Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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