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

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Article

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

The Journal of biological chemistry - 18 Nov 1994

Warriar N, Yu C, Govindan M V

Abstract excerpt

To determine the importance of specific amino acids in the hormone-binding domain of the human glucocorticoid receptor (hGR), we have generated mutants M565R, G567A, and A573Q. In hormone binding assays using [3H]cortisol, half-maximal saturation of dexamethasone competition was achieved at 10 pM...

Topics

Amino Acid Sequence
Antibodies
Base Sequence
Chloramphenicol O-Acetyltransferase
Hormones
Humans
Mammary Tumor Virus, Mouse
Molecular Sequence Data
Mutation
Oligodeoxyribonucleotides
Peptides
Precipitin Tests
Receptors, Glucocorticoid
Sequence Homology, Amino Acid
Transcriptional Activation

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Open in PubMed

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PMID: 7961865

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7961865-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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