3W0G

Crystal Structure of Rat VDR Ligand Binding Domain in Complex with Novel Nonsecosteroidal Ligands

Summary for 3W0G

• Entry DOI: 10.2210/pdb3w0g/pdb
• Related: 3W0H 3W0I 3W0J
• Descriptor: Vitamin D3 receptor, Mediator of RNA polymerase II transcription subunit 1, (2S)-3-{4-[2-(4-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}phenyl)propan-2-yl]phenoxy}propane-1,2-diol, ... (4 entities in total)
• Functional Keywords: gene regulation, transcription
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Nucleus: P13053 Q15648
• Total number of polymer chains: 2
• Total formula weight: 30728.45

Authors

Shimizu, T.,Asano, L.,Kuwabara, N.,Ito, I.,Waku, T.,Yanagisawa, J.,Miyachi, H. (deposition date: 2012-10-30, release date: 2013-10-09, Last modification date: 2023-11-08)

Primary citation

Asano, L.,Ito, I.,Kuwabara, N.,Waku, T.,Yanagisawa, J.,Miyachi, H.,Shimizu, T.
Structural basis for vitamin D receptor agonism by novel non-secosteroidal ligands.
Febs Lett., 587:957-963, 2013

PubMed Abstract: Non-secosteroidal ligands for vitamin D receptor (VDR) have been developed for the agonist with non-calcemic profiles. Here, we provide the structural mechanism of VDR agonism by novel non-secosteroidal ligands. All ligands had the similar efficacy, while two had the higher potency. Crystallographic analyses revealed that all ligands interacted with helix H10 and the loop between helices H6 and H7 in a similar manner, but also that the two ligands with higher potency had different interaction modes. This study suggests that distinct ligand potency depend upon differences in the formation and rearrangement of hydrogen-bond networks induced by each ligand.

PubMed: 23462137
DOI: 10.1016/j.febslet.2013.02.028

Experimental method

X-RAY DIFFRACTION (1.94 Å)