| pubmed-article:12124396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C0965644 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C1333897 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C1704838 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:12124396 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:12124396 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:12124396 | pubmed:dateCreated | 2002-8-7 | lld:pubmed |
| pubmed-article:12124396 | pubmed:abstractText | There is evidence that hypoxia-inducible factor-1alpha (HIF-1alpha) interacts with the tumor suppressor p53. To characterize the putative interaction, we mapped the binding of the core domain of p53 (p53c) to an array of immobilized HIF-1alpha-derived peptides and found two peptide-sequence motifs that bound to p53c with micromolar affinity in solution. One sequence was adjacent to and the other coincided with the two proline residues of the oxygen-dependent degradation domain (P402 and P564) that act as switches for the oxygen-dependent regulation of HIF-1alpha. The binding affinity was independent of the hydroxylation state of P564. We found from NMR spectroscopy that these sequence motifs bind to the DNA-binding site of p53c. Because the two sequences are homologous and separated by 120 residues, and one is in a largely unstructured transactivation domain, we speculate that each sequence motif in HIF-1alpha binds to a different subunit of the p53 tetramer, leading to very tight binding. The binding data support the proposal that p53 provides a route for the degradation in hypoxic tumor cells of HIF-1alpha that is not hydroxylated at the two proline residues. | lld:pubmed |
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| pubmed-article:12124396 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12124396 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12124396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12124396 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12124396 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12124396 | pubmed:author | pubmed-author:FershtAlan... | lld:pubmed |
| pubmed-article:12124396 | pubmed:author | pubmed-author:FriedlerAssaf... | lld:pubmed |
| pubmed-article:12124396 | pubmed:author | pubmed-author:HanssonLars... | lld:pubmed |
| pubmed-article:12124396 | pubmed:author | pubmed-author:FreundStefanS | lld:pubmed |
| pubmed-article:12124396 | pubmed:author | pubmed-author:RudigerStefan... | lld:pubmed |
| pubmed-article:12124396 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12124396 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:12124396 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12124396 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12124396 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12124396 | pubmed:pagination | 10305-9 | lld:pubmed |
| pubmed-article:12124396 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12124396 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12124396 | pubmed:articleTitle | Two sequence motifs from HIF-1alpha bind to the DNA-binding site of p53. | lld:pubmed |
| pubmed-article:12124396 | pubmed:affiliation | Cambridge Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, United Kingdom. | lld:pubmed |
| pubmed-article:12124396 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12124396 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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