2HCD

Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide

Summary for 2HCD

• Entry DOI: 10.2210/pdb2hcd/pdb
• Related: 1DB1 2HBH 2HC4
• Descriptor: Vitamin D receptor, SRC-1 from Nuclear receptor coactivator 1, 21-NOR-9,10-SECOCHOLESTA-5,7,10(19)-TRIENE-1,3,25-TRIOL, 20-(4-HYDROXY-4-METHYLPENTYL)-, (1A,3B,5Z,7E), ... (4 entities in total)
• Functional Keywords: alpha helical sandwich, gene regulation
• Biological source: Danio rerio (zebrafish); More
• Cellular location: Nucleus: Q9PTN2; Nucleus (By similarity): Q15788
• Total number of polymer chains: 2
• Total formula weight: 36339.51

Authors

Ciesielski, F.,Rochel, N.,Moras, D. (deposition date: 2006-06-16, release date: 2007-05-01, Last modification date: 2023-10-25)

Primary citation

Ciesielski, F.,Rochel, N.,Moras, D.
Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation
J.Steroid Biochem.Mol.Biol., 103:235-242, 2007

PubMed Abstract: 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.

PubMed: 17218092
DOI: 10.1016/j.jsbmb.2006.12.003

Experimental method

X-RAY DIFFRACTION (2.6 Å)