Structural highlights
Publication Abstract from PubMed
We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1alpha,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above.
Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands.,Demizu Y, Takahashi T, Kaneko F, Sato Y, Okuda H, Ochiai E, Horie K, Takagi K, Kakuda S, Takimoto-Kamimura M, Kurihara M Bioorg Med Chem Lett. 2011 Oct 15;21(20):6104-7. Epub 2011 Aug 17. PMID:21889334[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Demizu Y, Takahashi T, Kaneko F, Sato Y, Okuda H, Ochiai E, Horie K, Takagi K, Kakuda S, Takimoto-Kamimura M, Kurihara M. Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands. Bioorg Med Chem Lett. 2011 Oct 15;21(20):6104-7. Epub 2011 Aug 17. PMID:21889334 doi:10.1016/j.bmcl.2011.08.047
