The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.

By N. Rochel, J. Wurtz, A. Mitschler, Bruno P. Klaholz, D. Moras. Molecules and Cells, 2000

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How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Vitamin D and human health: lessons from vitamin D receptor null mice. (2008, neutral): “for crystallization with 1,25-(OH)2D (63).”
The nonskeletal effects of vitamin D: an Endocrine Society scientific statement. (2012, background): “The LBD for VDR has been crystallized, and its structure solved (13).”
Molecular Mechanisms of Vitamin D Action (2012, background): “The VDR LBD is a sandwich-like structure of at least 12 a-helices [22] presenting VDR surfaces for heterodimerization with RXR (predominantly helices [H] 9 and 10 and the loop between H8 and H9) as well as interaction with coactivators.”
Vitamin D Metabolism, Mechanism of Action, and Clinical Applications (2014, neutral): “One surprising result from crystallographic data is that different analogs did not appear to alter the configuration of the VDR (Rochel et al., 2000; Tocchini-Valentini et al., 2001).”
Noncalcemic actions of vitamin D receptor ligands. (2005, methodology): “The structure of the liganded VDR LBD (60) gives an opportunity to understand possible interactions between the natural ligand and the receptor.”