2hcd
|
Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide
OverviewOverview
The crystal structure of the ligand binding domain (LBD) of the wild-type, Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist, ligand with two identical side chains branching at carbon 20 reveals a, ligand-dependent structural rearrangement of the ligand binding pocket, (LBP). The rotation of a Leu side chain opens the access to a channel that, can accommodate the second side chain of the ligand. The 25% increase of, the LBP's volume does not alter the essential agonist features of VDR. The, possibility to adapt the LBP to novel ligands with different chemistry, and/or structure opens new perspectives in the design of more specifically, targeted ligands.
About this StructureAbout this Structure
2HCD is a Protein complex structure of sequences from Danio rerio with BIV as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation., Ciesielski F, Rochel N, Moras D, J Steroid Biochem Mol Biol. 2007 Mar;103(3-5):235-42. Epub 2007 Jan 10. PMID:17218092
Page seeded by OCA on Mon Nov 12 22:30:15 2007