Source:http://linkedlifedata.com/resource/pubmed/id/19807030
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2009-10-7
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pubmed:abstractText |
ETS proteins comprise a family of widespread transcription factors regulating expression of many animal genes. Structurally ETS proteins are characterized by conserved DNA-binding ETS domain, recognizing DNA sequences with trinucleotide GGA. Comparative analysis of structural features of ETS domain-DNA complexes was carried out and conserved contacts, important in terms of interaction stability and specificity were identified. The analysis revealed 9 conserved hydrogen bonds with DNA backbone phosphates and 2 conserved bidentate hydrogen bonds with DNA major groove atoms, one conserved hydrophobic cluster on protein-DNA interface, important for binding site recognition, and 12 conserved water molecules, possibly mediating ETS domain-DNA interaction. The results are represented in specialized data bank of protein-DNA complexes NPIDB.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0026-8984
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
666-74
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pubmed:meshHeading | |
pubmed:articleTitle |
[Conserved structural features of ETS domain--DNA complexes].
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pubmed:publicationType |
Journal Article,
Comparative Study,
English Abstract,
Research Support, Non-U.S. Gov't
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