Article
Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein.
Molecular endocrinology (Baltimore, Md.) - 1 Nov 1996
Weis K E, Ekena K, Thomas J A, Lazennec G, Katzenellenbogen B S
Abstract excerpt
To better understand structure-activity relationships in the human estrogen receptor (ER), we examined the role of tyrosine 537 in the transcriptional response of the receptor, since this residue is close to a region of the hormone-binding domain shown previously to be important in hormone-depend...
Topics
- Alanine
- Amino Acid Sequence
- Amino Acids
- Animals
- Binding Sites
- Breast Neoplasms
- CHO Cells
- Cricetinae
- Estradiol
- Histone Acetyltransferases
- Humans
- Molecular Sequence Data
- Mutation
- Nuclear Receptor Coactivator 1
- Phenotype
- Phosphorylation
- Receptors, Estrogen
- Recombinant Proteins