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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao The Journal of Stero...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
The Journal of Steroid Biochemistry and Molecular Biology
Article . 2004 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
HAL-Inserm
Article . 2004
Data sources: HAL-Inserm
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Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1α,25(OH)2D3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis

Authors: Ciesielski, Fabrice; Rochel, Natacha; Mitschler, André; Kouzmenko, Alexander; Moras, Dino;

Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1α,25(OH)2D3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis

Abstract

The nuclear receptor of Vitamin D can be activated by a large number of agonist molecules with a wide spectrum in their stereochemical framework. Up to now most of our structural information related to the protein-ligand complex formation is based on an engineered ligand binding domain (LBD) of the human receptor. We now have extended our database, using a wild-type LBD from zebrafish that confirms the previously reported results and allows to investigate the binding of ligands that induce significant conformational changes at the protein level.

Keywords

Models, Molecular, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Crystallography, X-Ray, Calcitriol, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Receptors, Calcitriol, Amino Acid Sequence, Zebrafish

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
61
Top 10%
Top 10%
Top 10%
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