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Steroids. 2001 Mar-May;66(3-5):213-21.

Central role of VDR conformations for understanding selective actions of vitamin D(3) analogues.

Author information

1
Institut für Physiologische Chemie I, Heinrich-Heine-Universität, Postfach 10 10 07, D-40001, Düsseldorf, Germany. carlberg@uni-duesseldorf.de

Abstract

The vitamin D(3) receptor (VDR) acts primarily as a heterodimer with the retinoid X receptor (RXR) on different types of 1alpha,25-dihydroxyvitamin D(3) (1alpha,25(OH)(2)D(3)) response elements (VDREs). Therefore, DNA-bound VDR-RXR heterodimers can be considered as the molecular switches of 1alpha,25(OH)(2)D(3) signalling. Functional conformations of the VDR within these molecular switches appear to be of central importance for describing the biologic actions of 1alpha,25(OH)(2)D(3) 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 1alpha,25(OH)(2)D(3) 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.

PMID:
11179728
DOI:
10.1016/s0039-128x(00)00150-1
[Indexed for MEDLINE]

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