Crystal Structure of the Vitamin D Nuclear Receptor Ligand Binding Domain in Complex with a Locked Side Chain Analog of Calcitriol.
From: Institut de Génétique et de Biologie Moléculaire et Cellulaire, Département de Biologie et de Génomique Structurales, Illkirch F-67400, France.
Archives of biochemistry and biophysics
- Publish Date: Apr 2007
- ISSN: 0003-9861
- Volume: 460
- Issue: 2
- Pages: 172-6
- Medium: Print
- Language: English
- Citation (JAMA): Rochel Natacha, Hourai Shinji, Pérez-García Xenxo, et al. Crystal Structure of the Vitamin D Nuclear Receptor Ligand Binding Domain in Complex with a Locked Side Chain Analog of Calcitriol.. Arch. Biochem. Biophys. Apr 2007;460:172-6
Abstract
The crystal structures of vitamin D nuclear receptor (VDR) have revealed that all compounds are anchored by the same residues to the ligand binding pocket (LBP). Based on this observation, a synthetic analog with a locked side chain (21-nor-calcitriol-20(22),23-diyne) has been synthesized in order to gain in entropy energy with a predefined active side chain conformation. The crystal structure of VDR LBD bound to this locked side chain analogue while confirming the docking provides a structural basis for the activity of this compound.
Mesh Headings (Keywords): Binding Sites, Calcitriol, Entropy, Humans, Ligands, Protein Binding, Protein Structure, Tertiary, Receptors, Calcitriol, Structure-Activity Relationship
Check for Full Text / PubMed Unique Identifier (PMID): 17346665
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