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Journal Articles Acta crystallographica Section F : Structural biology communications [2014-...] Year : 2008

Nuclear receptor ligand-binding domains: reduction of helix H12 dynamics to favour crystallization.

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Abstract

Crystallization trials of the human retinoid X receptor alpha ligand-binding domain (RXRalpha LBD) in complex with various ligands have been carried out. Using fluorescence anisotropy, it has been found that when compared with agonists these small-molecule effectors enhance the dynamics of the RXRalpha LBD C-terminal helix H12. In some cases, the mobility of this helix could be dramatically reduced by the addition of a 13-residue co-activator fragment (CoA). In keeping with these observations, crystals have been obtained of the corresponding ternary RXRalpha LBD-ligand-CoA complexes. In contrast, attempts to crystallize complexes with a highly mobile H12 remained unsuccessful. These experimental observations substantiate the previously recognized role of co-regulator fragments in facilitating the crystallization of nuclear receptor LBDs.

Dates and versions

inserm-00350909 , version 1 (03-02-2009)

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Cite

Virginie Nahoum, Alexandra Lipski, Fabien Quillard, Jean François Guichou, Yvan Boublik, et al.. Nuclear receptor ligand-binding domains: reduction of helix H12 dynamics to favour crystallization.. Acta crystallographica Section F : Structural biology communications [2014-..], 2008, 64 (Pt 7), pp.614-6. ⟨10.1107/S1744309108015492⟩. ⟨inserm-00350909⟩
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