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Article

Residues of the human nuclear vitamin D receptor that form hydrogen bonding interactions with the three hydroxyl groups of 1alpha,25-dihydroxyvitamin D3.

The Journal of steroid biochemistry and molecular biology - 1 Mar 2007

Reddy Madhuri D, Stoynova Ludmilla, Acevedo Alejandra, Collins Elaine D

Abstract excerpt

Most of the biological effects of 1,25-dihydroxyvitamin D(3) (hormone D) are mediated through the nuclear vitamin D receptor (VDR). Hormone binding induces conformational changes in VDR that enable the receptor to activate gene transcription. It is known that residues S237 and R274 form hydrogen bonds with the 1-hydroxyl group of hormone D, while residues Y143 and S278, and residues H305 and H397 form hydrogen...

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Gene Expression Regulation
Hydrogen Bonding
Hydroxylation
Ligands
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Calcitriol

Transcriptional Activation

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Identifiers

PMID: 17257828
DOI: 10.1016/j.jsbmb.2006.12.045

Genes

VDR

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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