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Molecules 2015, 20(11), 20473-20486; doi:10.3390/molecules201119713

Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling

1
Medical College, China Three Gorges University, 8 Daxue Road, Xiling District, Yichang 443002, China
2
Hubei Key Laboratory of Tumor Microenvironment and Immunotherapy, China Three Gorges University, 8 Daxue Road, Xiling District, Yichang 443002, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 8 October 2015 / Revised: 2 November 2015 / Accepted: 11 November 2015 / Published: 18 November 2015
(This article belongs to the Section Bioorganic Chemistry)
View Full-Text   |   Download PDF [875 KB, uploaded 18 November 2015]   |  

Abstract

Vitamin D Receptor (VDR) belongs to the nuclear receptor (NR) superfamily. Whereas the structure of the ligand binding domain (LBD) of VDR has been determined in great detail, the role of its amino acid residues in stabilizing the structure and ligand triggering conformational change is still under debate. There are 13 α-helices and one β-sheet in the VDR LBD and they form a three-layer sandwich structure stabilized by 10 residues. Thirty-six amino acid residues line the ligand binding pocket (LBP) and six of these residues have hydrogen-bonds linking with the ligand. In 1α,25-dihydroxyvitamin D3 signaling, H3 and H12 play an important role in the course of conformational change resulting in the provision of interfaces for dimerization, coactivator (CoA), corepressor (CoR), and hTAFII 28. In this paper we provide a detailed description of the amino acid residues stabilizing the structure and taking part in conformational change of VDR LBD according to functional domains. View Full-Text
Keywords: ligand binding domain; vitamin D receptor; structure basis; functional domains; conformational change ligand binding domain; vitamin D receptor; structure basis; functional domains; conformational change
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Wan, L.-Y.; Zhang, Y.-Q.; Chen, M.-D.; Du, Y.-Q.; Liu, C.-B.; Wu, J.-F. Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling. Molecules 2015, 20, 20473-20486.

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