Source:http://linkedlifedata.com/resource/pubmed/id/18189286
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2008-4-2
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| pubmed:abstractText |
Peptides are valuable tools for studying protein-protein interactions, especially in cases of isolated protein domains and natively unfolded proteins. Here, we used peptides to quantitatively characterize the interaction between the natively unfolded HIV-1 Tat protein and the tetramerization domain of the cellular tumor suppressor protein p53. We used peptide mapping, fluorescence anisotropy, and NMR spectroscopy to perform a detailed structural and biophysical characterization of the interaction between the two proteins and elucidate its molecular mechanism, which have so far been studied using cell-based methods. We show that the p53 tetramerization domain, p53(326-355), binds directly to residues 1-35 and 47-57 in Tat. We have characterized the interaction between p53(326-355) and Tat(47-57) in detail. The p53 residues that are mainly involved in binding to Tat(47-57) are E343 and E349, which bind to the positively charged arginine-rich motif of Tat by a partly electrostatic mechanism. All oligomerization states of p53(326-355) bind Tat(47-57) without inhibiting p53 tetramerization, since the residues in p53(326-355) that bind Tat(47-57) face away from the tetramerization interface. We conclude that p53 is able to bind Tat as a transcriptionally active tetramer.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:issn |
0006-3525
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
90
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
105-16
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:18189286-Alanine,
pubmed-meshheading:18189286-Amino Acid Motifs,
pubmed-meshheading:18189286-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:18189286-Gene Products, tat,
pubmed-meshheading:18189286-HIV-1,
pubmed-meshheading:18189286-Models, Molecular,
pubmed-meshheading:18189286-Molecular Sequence Data,
pubmed-meshheading:18189286-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:18189286-Osmolar Concentration,
pubmed-meshheading:18189286-Peptide Fragments,
pubmed-meshheading:18189286-Protein Binding,
pubmed-meshheading:18189286-Protein Structure, Quaternary,
pubmed-meshheading:18189286-Protein Structure, Tertiary,
pubmed-meshheading:18189286-Static Electricity,
pubmed-meshheading:18189286-Temperature,
pubmed-meshheading:18189286-Tumor Suppressor Protein p53
|
| pubmed:year |
2008
|
| pubmed:articleTitle |
Using peptides to study the interaction between the p53 tetramerization domain and HIV-1 Tat.
|
| pubmed:affiliation |
Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem 91904, Israel.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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