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Ligand specificity and conformational dependence of the hepatic nuclear factor-4alpha (HNF-4alpha ).

Authors: Petrescu, AD  Hertz, R  Bar-Tana, J  Schroeder, F  Kier, AB 
Citation: Petrescu AD, etal., J Biol Chem 2002 Jul 5;277(27):23988-99.
Pubmed: (View Article at PubMed) PMID:11940586
DOI: Full-text: DOI:10.1074/jbc.M201241200

Hepatic nuclear factor-4alpha (HNF-4alpha) controls the expression of genes encoding proteins involved in lipid and carbohydrate metabolism. Fatty acyl-CoA thioesters have recently been proposed to be naturally occurring ligands of HNF-4alpha and to regulate its transcriptional activity as function of their chain length and degree of unsaturation (Hertz, R., Magenheim, J., Berman, I., and Bar-Tana, J. (1998) Nature 392, 512-516). However, the apparent low affinities (microm K(d) values) obtained with a radiolabeled fatty acyl-CoA ligand binding assay raised questions regarding the physiological significance of this finding. Furthermore, it is not known whether interaction with fatty acyl-CoA alters the structure of HNF-4alpha. These issues were examined using rat recombinant HNF-4alpha ligand-binding domain (HNF-4alphaLBD) in conjunction with photon counting fluorescence and circular dichroism. First, fluorescence resonance energy transfer between HNF-4alphaLBD tryptophan (Trp) and cis-parinaroyl-CoA yielded an intermolecular distance of

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RGD Object Information
RGD ID: 625581
Created: 2002-10-04
Species: All species
Last Modified: 2002-10-04
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.