Hormone receptor ligand-binding domains

Nuclear Hormone Receptors Ligand Binding Domains... 

Tab. 1.1 PDB codes of all nuclear hormone receptor-ligand-binding domains in the protein data bank as of December 2002.

Instead of adopting this approach, we decided to control the activity of a protein through its fusion to a steroid hormone receptor ligand binding domain. In absence of its ligand, the receptor forms a cytoplasmic complex... 

Simons SS Jr. Structure and function of the steroid and nuclear receptor ligand-binding domain. In The Molecular Biology of Steroid and Nuclear Hormone Receptors. Freedman LP, ed. 1998. Birkhauser, Boston, pp. 35-104. 

Valentine, J.E., KaUdioven, E., White, R., Hoare, S., and Parker, M.G., Mutations in the estrogen receptor ligand binding domain discriminate between hormone-dependent transactivation and transrepression, J. Biol Chem., 275,25322-25329,2000. 

Figure 4.20 Tyrosine kinase-linked receptors (a) those with inherentTK activity insulin receptor. The intracellular tail and cytoplasmic proteins become phosphoryLated following hormone engagement with the ligand-binding domain...

Protein receptors for endogenous ligands (e.g., hormones, neurotransmitters) share some common properties. They contain a ligand-binding domain, where the hormone or neurotransmitter attaches, and an effector domain, which translates the binding into some from of action. 

The use of structure-based virtual screening toward novel nuclear hormone receptor antagonists was described by Schapira et al. [263]. As only X-ray structures of ligand binding domains of agonist-bound nuclear receptors with exception of the antagonist-bound estrogen receptor-a are available, the authors constructed an inactive ... 

The receptor protein (52 kDa) is a member of the steroid hormone receptor superfamily, which has a DNA-binding as well as ligand-binding domain. Another receptor, the retinoid X receptor is also involved, and after binding of the peroxisome proliferator, the two receptors form a heterodimer. This binds to a regulatory DNA sequence known as the peroxisome proliferator response element. The end result of the interaction between peroxisome proliferators and this system is that genes are switched on, leading to increases in synthesis (induction) of both microsomal and peroxisomal enzymes and possibly hyperplasia. 

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