(Q54100959)

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Conformational change in the human glucocorticoid receptor induced by ligand binding is altered by mutation of isoleucine 747 by a threonine.

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Conformational change in the human glucocorticoid receptor induced by ligand binding is altered by mutation of isoleucine 747 by a threonine. (English)

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

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Roux S

1

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Térouanne B

2

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Couette B

3

1 reference

Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Rafestin-Oblin ME

4

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Nicolas JC

5

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

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1 April 1999

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

274

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

15

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

10059-10065

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Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

Gene regulation by steroid hormones

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The steroid and thyroid hormone receptor superfamily

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Nuclear receptors enhance our understanding of transcription regulation

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Steroid and related receptors

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In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus

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Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90.

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Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region

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A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor).

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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

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Molecular basis of agonism and antagonism in the oestrogen receptor

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Ligand-dependent conformational changes in the progesterone receptor are necessary for events that follow DNA binding

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Ligand-induced conformational change in the human mineralocorticoid receptor occurs within its hetero-oligomeric structure.

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Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping

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Mechanism of antiandrogen action: conformational changes of the receptor.

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Steroid-induced conformational changes at ends of the hormone-binding domain in the rat glucocorticoid receptor are independent of agonist versus antagonist activity.

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Distinct conformational changes induced by 20-epi analogues of 1 alpha,25-dihydroxyvitamin D3 are associated with enhanced activation of the vitamin D receptor

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Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis.

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Distinct binding determinants for 9-cis retinoic acid are located within AF-2 of retinoic acid receptor alpha

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Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance

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A mutation of the glucocorticoid receptor in primary cortisol resistance

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A somatic cell genetic method for identification of untargeted mutations in the glucocorticoid receptor that cause hormone binding deficiencies

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Co-activators and co-repressors in the integration of transcriptional responses

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Reconstitution of progesterone receptor with heat shock proteins

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Primary structure and expression of a functional human glucocorticoid receptor cDNA

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Altered ligand binding properties and enhanced stability of a constitutively active estrogen receptor: evidence that an open pocket conformation is required for ligand interaction.

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Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability

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The nuclear receptor ligand-binding domain: structure and function

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AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors

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Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription

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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily

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Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state

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Identifiers

10.1074/JBC.274.15.10059

1 reference

Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 May 2018

http://europepmc.org/abstract/MED/10187785

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