| pubmed-article:14668441 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C0030125 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1512424 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:14668441 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:14668441 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:14668441 | pubmed:dateCreated | 2003-12-24 | lld:pubmed |
| pubmed-article:14668441 | pubmed:abstractText | Biological responses to oxygen availability play important roles in development, physiological homeostasis, and many disease processes. In mammalian cells, this adaptation is mediated in part by a conserved pathway centered on the hypoxia-inducible factor (HIF). HIF is a heterodimeric protein complex composed of two members of the basic helix-loop-helix Per-ARNT-Sim (PAS) (ARNT, aryl hydrocarbon receptor nuclear translocator) domain family of transcriptional activators, HIFalpha and ARNT. Although this complex involves protein-protein interactions mediated by basic helix-loop-helix and PAS domains in both proteins, the role played by the PAS domains is poorly understood. To address this issue, we have studied the structure and interactions of the C-terminal PAS domain of human HIF-2alpha by NMR spectroscopy. We demonstrate that HIF-2alpha PAS-B binds the analogous ARNT domain in vitro, showing that residues involved in this interaction are located on the solvent-exposed side of the HIF-2alpha central beta-sheet. Mutating residues at this surface not only disrupts the interaction between isolated PAS domains in vitro but also interferes with the ability of full-length HIF to respond to hypoxia in living cells. Extending our findings to other PAS domains, we find that this beta-sheet interface is widely used for both intra- and intermolecular interactions, suggesting a basis of specificity and regulation of many types of PAS-containing signaling proteins. | lld:pubmed |
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| pubmed-article:14668441 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14668441 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668441 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14668441 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14668441 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14668441 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14668441 | pubmed:author | pubmed-author:GardnerKevin... | lld:pubmed |
| pubmed-article:14668441 | pubmed:author | pubmed-author:BruickRichard... | lld:pubmed |
| pubmed-article:14668441 | pubmed:author | pubmed-author:ErbelPaul J... | lld:pubmed |
| pubmed-article:14668441 | pubmed:author | pubmed-author:CardPaul BPB | lld:pubmed |
| pubmed-article:14668441 | pubmed:author | pubmed-author:KarakuzuOzgur... | lld:pubmed |
| pubmed-article:14668441 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14668441 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:14668441 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:14668441 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14668441 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14668441 | pubmed:pagination | 15504-9 | lld:pubmed |
| pubmed-article:14668441 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:14668441 | pubmed:meshHeading | pubmed-meshheading:14668441... | lld:pubmed |
| pubmed-article:14668441 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14668441 | pubmed:articleTitle | Structural basis for PAS domain heterodimerization in the basic helix--loop--helix-PAS transcription factor hypoxia-inducible factor. | lld:pubmed |
| pubmed-article:14668441 | pubmed:affiliation | Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA. | lld:pubmed |
| pubmed-article:14668441 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14668441 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
