Article
A role for helix 3 of the TRbeta ligand-binding domain in coactivator recruitment identified by characterization of a third cluster of mutations in resistance to thyroid hormone.
The EMBO journal - 17 Aug 1998
Collingwood T N, Wagner R, Matthews C H, Clifton-Bligh R J, Gurnell M, Rajanayagam O, Agostini M, Fletterick R J, Beck-Peccoz P, Reinhardt W, Binder G, Ranke M B, Hermus A, Hesch R D, Lazarus J, Newrick P, Parfitt V, Raggatt P, de Zegher F, Chatterjee V K
Abstract excerpt
Resistance to thyroid hormone (RTH) has hitherto been associated with thyroid hormone beta receptor (TRbeta) mutations which cluster in two regions (alphaalpha 310-353 and alphaalpha 429-461) of the hormone-binding domain and closely approximate the ligand-binding cavity. Here, we describe a thir...
Topics
- Amino Acid Sequence
- Cell Line
- Dimerization
- Genes, Dominant
- Genotype
- Humans
- Ligands
- Molecular Sequence Data
- Mutation
- Phenotype