title: Structure-function relationships of the chicken progesterone receptor.
abstract: To define the functional domains of the chicken progesterone receptor (CPR) and to establish the origin of the receptor A and B proteins, we have cloned and sequenced the complete cDNA encoding the CPR. The receptor A and B proteins arise by alternate initiation of translation from a single mRNA transcript. Using deletion mutants in the receptor A cDNA, we have determined that the DNA binding and gene activator regions reside in the central portion of the protein, while the hormone binding domain is located in the C-terminal region. The target gene activator site of the receptor is modulated by interaction with the hormone binding domain.
authors: Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.
authors: O M
authors: OM
authors: Conneely
authors: A D
authors: AD
authors: Dobson
authors: M A
authors: MA
authors: Carson
authors: B L
authors: BL
authors: Maxwell
authors: M J
authors: MJ
authors: Tsai
authors: W T
authors: WT
authors: Schrader
authors: B W
authors: BW
authors: O'Malley
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D002645:Chickens; D004247:DNA / Q000235:genetics; D000939:Epitopes / Q000032:analysis; D005796:Genes; D006801:Humans; D011980:Receptors, Progesterone / Q000235:genetics* / Q000276:immunology; D011988:Receptors, Thyroid Hormone / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
chemical_list: D000911:Antibodies, Monoclonal; D000939:Epitopes; D011980:Receptors, Progesterone; D011988:Receptors, Thyroid Hormone; D004247:DNA