Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgen-independent prostate cancer.

Journal of medicinal chemistry - 28 Mar 2002

Matias Pedro M, Carrondo Maria Arménia, Coelho Ricardo, Thomaz Monica, Zhao Xiao-Yan, Wegg Anja, Crusius Kerstin, Egner Ursula, Donner Peter

Abstract excerpt

The crystal structure of a mutant androgen receptor (AR) ligand-binding domain (LBD) in complex with the agonist 9alpha-fluorocortisol has been determined at 1.95 A resolution. This mutant AR contains two mutations (L701H and T877A) and was previously reported as a high-affinity cortisol/cortison...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-Inflammatory Agents
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucocorticoids

Share to Hydrogen Bonding

Share to Ligands

Share to Models, Chemical

Share to Prostatic Neoplasms

Share to Receptors, Androgen

Source

Identifiers

PMID: 11906285
DOI: 10.1021/jm011072j

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11906285-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgen-independent prostate cancer.PMID 11906285Read ↗

A glucocorticoid-responsive mutant androgen receptor exhibits unique ligand specificity: therapeutic implications for androgen-independent prostate cancer.Semantic proximity Read ↗

Androgen receptor mutations modulate activation by 11-oxygenated androgens and glucocorticoids.Semantic proximity Read ↗

Systematic structure-function analysis of androgen receptor Leu701 mutants explains the properties of the prostate cancer mutant L701H.Semantic proximity Read ↗

Glucocorticoids manifest androgenic activity in a cell line derived from a metastatic prostate cancer.Semantic proximity Read ↗

The ligand-dependent interaction of mineralocorticoid receptor with coactivator and corepressor peptides suggests multiple activation mechanisms.Semantic proximity Read ↗

Structural Analysis on the Pathologic Mutant Glucocorticoid Receptor Ligand-Binding Domains.Semantic proximity Read ↗

A novel adrenocorticotropin receptor mutation alters its structure and function, causing familial glucocorticoid deficiency.Semantic proximity Read ↗

Molecular dynamics simulations reveal the plausible agonism/antagonism mechanism by steroids on androgen receptor mutations.Semantic proximity Read ↗

A critical region in the mineralocorticoid receptor for aldosterone binding and activation by cortisol: evidence for a common mechanism governing ligand binding specificity in steroid hormone receptors.Semantic proximity Read ↗

Hormone binding domain of human glucocorticoid receptor. Enhancement of transactivation function by substitution mutants M565R and A573Q.Semantic proximity Read ↗

Backbone 1H, 13C, and 15N resonance assignments of the ligand binding domain of the human wildtype glucocorticoid receptor and the F602S mutant variant.Semantic proximity Read ↗

Antimineralocorticoid 11beta-substituted spirolactones exhibit androgen receptor agonistic activity: a structure function study.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.