2HBH

Crystal structure of Vitamin D nuclear receptor ligand binding domain bound to a locked side-chain analog of calcitriol and SRC-1 peptide

Summary for 2HBH

• Entry DOI: 10.2210/pdb2hbh/pdb
• Related: 1DB1 2HC4 2HCD
• Descriptor: Vitamin D receptor, SRC-1 from Nuclear receptor coactivator 1, 1,3-CYCLOHEXANEDIOL, 4-METHYLENE-5-[(2E)-[(1S,3AS,7AS)-OCTAHYDRO-1-(5-HYDROXY-5-METHYL-1,3-HEXADIYNYL)-7A-METHYL-4H-INDEN-4-YLIDENE]ETHYLIDENE]-, (1R,3S,5Z), ... (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: 36231.29

Authors

Rochel, N.,Hourai, S.,Moras, D. (deposition date: 2006-06-14, release date: 2007-05-01, Last modification date: 2023-10-25)

Primary citation

Rochel, N.,Hourai, S.,Perez-Garcia, X.,Rumbo, A.,Mourino, A.,Moras, D.
Crystal structure of the vitamin D nuclear receptor ligand binding domain in complex with a locked side chain analog of calcitriol
Arch.Biochem.Biophys., 460:172-176, 2007

PubMed 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.

PubMed: 17346665
DOI: 10.1016/j.abb.2007.01.031

Experimental method

X-RAY DIFFRACTION (2.65 Å)