Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition.

By R. Bledsoe, V. Montana, Thomas B. Stanley, C. Delves, C. Apolito, D. D. Mckee, Thomas G. Consler, Derek J. Parks, E. Stewart, T. Willson and 4 more. Cell, 2002

792 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology, Pharmacology

View Paper: https://www.semanticscholar.org/paper/5eae793020ee6fe9de42826698d19240b2f08bc8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

1. P. Barnes
2. J. Cidlowski

In Molecular Biology

1. P. Barnes
2. Bart Staels
3. W. Vanden Berghe
4. G. Haegeman
5. K. De Bosscher
6. S. Swallow

In Pharmacology

1. S. Swallow

Citations in the corpus

• Overview of Nomenclature of Nuclear Receptors (2006, background): “In RARs and GR, this conformation is stabilized by hydrophobic interactions with the bound activating ligand (Bledsoe et al., 2002; Germain et al., 2004).”
• Fluorine in medicinal chemistry. (2015, background): “The 3,5-dimethyl analogue (107) proved to be 20- and 100-fold more potent than the 3-methyl and Figure 66 Structure of dexamethasone bound to the glucocorticoid receptor (PDB entry: 1M2Z) [110,111] showing close contacts of 11β-OH and 9α-F.”
• How corticosteroids control inflammation: Quintiles Prize Lecture 2005 (2006, background): “The recent resolution of the crystal structure of the ligand binding domain of GR may help in better design of dissociated steroids (Bledsoe et al., 2002).”
• The interplay between the glucocorticoid receptor and nuclear factor-kappaB or activator protein-1: molecular mechanisms for gene repression. (2003, background): “Structural comparisons of GR, AR, PR, and ER start to provide insight into how functional specificity is achieved, because many subtle differences in the secondary structure and the topology of their ligand-binding pockets exist in these steroid receptors (364).”
• The Biology of the Glucocorticoid Receptor: New Signaling Mechanisms in Health and Disease (2013, background): “The LBD, consisting of 12 α-helices and four β-sheets, forms a hydrophobic pocket for binding glucocorticoids and also contains an activation function (AF2) that interacts with coregulators in a ligand-dependent manner (18).”