Article
Ternary complex of human RORγ ligand-binding domain, inverse agonist and SMRT peptide shows a unique mechanism of corepressor recruitment.
Genes to cells : devoted to molecular & cellular mechanisms - 1 Jun 2017
Noguchi Masato, Nomura Akihiro, Murase Ken, Doi Satoki, Yamaguchi Keishi, Hirata Kazuyuki, Shiozaki Makoto, Hirashima Shintaro, Kotoku Masayuki, Yamaguchi Takayuki, Katsuda Yoshiaki, Steensma Ruo, Li Xioalin, Tao Haiyan, Tse Bruno, Fenn Morgan, Babine Robert, Bradley Erin, Crowe Paul, Thacher Scott, Adachi Tsuyoshi, Kamada Masafumi
Abstract excerpt
Retinoid-related orphan receptor gamma (RORγ) directly controls the differentiation of Th17 cell and the production of interleukin-17, which plays an integral role in autoimmune diseases. To obtain insight into RORγ, we have determined the first crystal structure of a ternary complex containing RORγ ligand-binding domain (LBD) bound with a novel synthetic inhibitor and a repressor peptide, 22-mer peptide from...
Topics
- Binding Sites
- Humans
- Hydrogen Bonding
- Models, Molecular
- Mutation
- Nuclear Receptor Co-Repressor 2
- Nuclear Receptor Coactivator 1
- Nuclear Receptor Subfamily 1, Group F, Member 3