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Central role of VDR conformations for understanding selective actions of vitamin D3 analogues

Identifieur interne : 000A50 ( Main/Exploration ); précédent : 000A49; suivant : 000A51

Central role of VDR conformations for understanding selective actions of vitamin D3 analogues

Auteurs : Carsten Carlberg [Allemagne] ; Marcus Quack [Allemagne] ; Michaela Herdick [Allemagne] ; Yvonne Bury [Allemagne] ; Patsie Polly [Allemagne] ; Andrea Toell [Allemagne]

Source :

RBID : ISTEX:BF594BD05AF28D39293AB85B9ABB003FA478187E

Mots-clés :

Abstract

The vitamin D3 receptor (VDR) acts primarily as a heterodimer with the retinoid X receptor (RXR) on different types of 1α,25-dihydroxyvitamin D3 (1α,25(OH)2D3) response elements (VDREs). Therefore, DNA-bound VDR-RXR heterodimers can be considered as the molecular switches of 1α,25(OH)2D3 signalling. Functional conformations of the VDR within these molecular switches appear to be of central importance for describing the biologic actions of 1α,25(OH)2D3 and its analogues. Moreover, VDR conformations provide a molecular basis for understanding the potential selective profile of VDR agonists, which is critical for a therapeutic application. This review discusses VDR conformations and their selective stabilization by 1α,25(OH)2D3 and its analogues, such as EB1089 and Gemini, as a monomer in solution or as a heterodimer with RXR bound to different VDREs and complexed with coactivator or corepressor proteins.


Url:
DOI: 10.1016/S0039-128X(00)00150-1


Affiliations:


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<div type="abstract" xml:lang="en">The vitamin D3 receptor (VDR) acts primarily as a heterodimer with the retinoid X receptor (RXR) on different types of 1α,25-dihydroxyvitamin D3 (1α,25(OH)2D3) response elements (VDREs). Therefore, DNA-bound VDR-RXR heterodimers can be considered as the molecular switches of 1α,25(OH)2D3 signalling. Functional conformations of the VDR within these molecular switches appear to be of central importance for describing the biologic actions of 1α,25(OH)2D3 and its analogues. Moreover, VDR conformations provide a molecular basis for understanding the potential selective profile of VDR agonists, which is critical for a therapeutic application. This review discusses VDR conformations and their selective stabilization by 1α,25(OH)2D3 and its analogues, such as EB1089 and Gemini, as a monomer in solution or as a heterodimer with RXR bound to different VDREs and complexed with coactivator or corepressor proteins.</div>
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