Format:
Online-Ressource
ISSN:
1469-3178
Content:
Nuclear receptors (NRs) are ligand‐dependent transcription factors that control a large number of physiological events through the regulation of gene transcription. NRs function either as homodimers or as heterodimers with retinoid X receptor/ultraspiracle protein (RXR/USP). A structure‐based sequence analysis aimed at discovering the molecular mechanism that controls the dimeric association of the ligand‐binding domain reveals two sets of differentially conserved residues, which partition the entire NR superfamily into two classes related to their oligomeric behaviour. Site‐directed mutagenesis confirms the functional importance of these residues for the dimerization process and/or transcriptional activity. All homodimers belong to class I, in which the related residues contribute a communication pathway of two salt bridges linking helix 1 on the cofactor‐binding site to the dimer interface. A salt bridge involving a differentially conserved arginine residue in loop H8–H9 defines the signature motif of heterodimers. RXR/USP and all Caenorhabditis elegans NRs belong to class I, supporting the hypothesis of an earlier emergence of this class.
In:
volume:5
In:
number:4
In:
year:2004
In:
pages:423-429
In:
extent:7
In:
European Molecular Biology Organization, EMBO reports, Heidelberg : EMBO Press, [200]-, 5, Heft 4 (2004), 423-429 (gesamt 7), 1469-3178
Language:
English
DOI:
10.1038/sj.embor.7400119
URN:
urn:nbn:de:101:1-2023092808031834471568
URL:
https://doi.org/10.1038/sj.embor.7400119
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023092808031834471568
URL:
https://d-nb.info/1304241750/34
URL:
https://doi.org/10.1038/sj.embor.7400119
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