| Literature DB >> 7501015 |
R L Wagner1, J W Apriletti, M E McGrath, B L West, J D Baxter, R J Fletterick.
Abstract
The crystal structure of the rat alpha 1 thyroid hormone receptor ligand-binding domain bound with a thyroid hormone agonist reveals that ligand is completely buried within the domain as part of the hydrophobic core. In addition, the carboxy-terminal activation domain forms an amphipathic helix, with its hydrophobic face constituting part of the hormone binding cavity. These observations suggest a structural role for ligand, in establishing the active conformation of the receptor, that is likely to underlie hormonal regulation of gene expression for the nuclear receptors.Entities:
Mesh：
Substances：
Year: 1995 PMID： 7501015 DOI： 10.1038/378690a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962