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Article

The unique tryptophan residue of the vitamin D receptor is critical for ligand binding and transcriptional activation.

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research - 1 Jan 2001

Solomon C, Macoritto M, Gao X L, White J H, Kremer R

Abstract excerpt

The human vitamin D receptor (hVDR) is a member of the nuclear receptor superfamily of transcriptional regulators. Here we show that tryptophan 286 of the hVDR is critical for ligand binding and transactivation of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] target genes. Two mutants of the hVDR were p...

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Share to Dimerization
Share to Histone Acetyltransferases
Share to Nuclear Receptor Coactivator 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Receptors, Calcitriol

Share to Receptors, Retinoic Acid

Share to Retinoid X Receptors

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Source

Identifiers

PMID: 11149488
DOI: 10.1359/jbmr.2001.16.1.39

Genes

SRC
VDR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-11149488-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

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