A report on Estrogen receptor and Elwood V. Jensen

A dimer of the ligand-binding region of ERβ (PDB rendering based on ).
The domain structures of ERα and ERβ, including some of the known phosphorylation sites involved in ligand-independent regulation.
A dimer of the ligand-binding region of ERα (PDB rendering based on ).
Nolvadex (tamoxifen) 20 mg
Arimidex (anastrozole) 1 mg

In 2004 he received the Albert Lasker Award for Basic Medical Research for his research on estrogen receptors.

- Elwood V. Jensen

Estrogen receptors were first identified by Elwood V. Jensen at the University of Chicago in 1958, for which Jensen was awarded the Lasker Award.

- Estrogen receptor
A dimer of the ligand-binding region of ERβ (PDB rendering based on ).

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Crystallographic structure of a heterodimer of the nuclear receptors PPAR-γ (green) and RXR-α (cyan) bound to double stranded DNA (magenta) and two molecules of the NCOA2 coactivator (red). The PPAR-γ antagonist GW9662 and RXR-α agonist retinoic acid are depicted as space-filling models (carbon = white, oxygen = red, nitrogen = blue, chlorine = green).

Nuclear receptor

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In the field of molecular biology, nuclear receptors are a class of proteins responsible for sensing steroids, thyroid hormones, cholesterol, and vitamins.

In the field of molecular biology, nuclear receptors are a class of proteins responsible for sensing steroids, thyroid hormones, cholesterol, and vitamins.

Crystallographic structure of a heterodimer of the nuclear receptors PPAR-γ (green) and RXR-α (cyan) bound to double stranded DNA (magenta) and two molecules of the NCOA2 coactivator (red). The PPAR-γ antagonist GW9662 and RXR-α agonist retinoic acid are depicted as space-filling models (carbon = white, oxygen = red, nitrogen = blue, chlorine = green).
Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.
Mechanism of class I nuclear receptor action. A class I nuclear receptor (NR), in the absence of ligand, is located in the cytosol. Hormone binding to the NR triggers dissociation of heat shock proteins (HSP), dimerization, and translocation to the nucleus, where the NR binds to a specific sequence of DNA known as a hormone response element (HRE). The nuclear receptor DNA complex in turn recruits other proteins that are responsible for transcription of downstream DNA into mRNA, which is eventually translated into protein, which results in a change in cell function.
Mechanism of class II nuclear receptor action. A class II nuclear receptor (NR), regardless of ligand-binding status, is located in the nucleus bound to DNA. For the purpose of illustration, the nuclear receptor shown here is the thyroid hormone receptor (TR) heterodimerized to the RXR. In the absence of ligand, the TR is bound to corepressor protein. Ligand binding to TR causes a dissociation of corepressor and recruitment of coactivator protein, which, in turn, recruits additional proteins such as RNA polymerase that are responsible for transcription of downstream DNA into RNA and eventually protein.
Structural basis for the mechanism of nuclear receptor agonist and antagonist action. The structures shown here are of the ligand binding domain (LBD) of the estrogen receptor (green cartoon diagram) complexed with either the agonist diethylstilbestrol (top, ) or antagonist 4-hydroxytamoxifen (bottom, ). The ligands are depicted as space filling spheres (white = carbon, red = oxygen). When an agonist is bound to a nuclear receptor, the C-terminal alpha helix of the LDB (H12; light blue) is positioned such that a coactivator protein (red) can bind to the surface of the LBD. Shown here is just a small part of the coactivator protein, the so-called NR box containing the LXXLL amino acid sequence motif. Antagonists occupy the same ligand binding cavity of the nuclear receptor. However antagonist ligands in addition have a sidechain extension which sterically displaces H12 to occupy roughly the same position in space as coactivators bind. Hence coactivator binding to the LBD is blocked.
Phylogenetic tree of human nuclear receptors

Type I nuclear receptors include members of subfamily 3, such as the androgen receptor, estrogen receptors, glucocorticoid receptor, and progesterone receptor.

1958 – Elwood Jensen – isolated the estrogen receptor