Structural recognitions in the interactions of androgens and receptor proteins and in their association with nuclear acceptor components
| Autor: | Shutsung Liao, Tehming Liang, J. L. Tymoczko |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
Male
Cytoplasm Protein Conformation Estranes Polynucleotides Molecular Conformation Receptors Cell Surface Plasma protein binding Cytoplasmic receptor Biochemistry Structure-Activity Relationship Endocrinology Protein structure Microsomes Animals Receptor Nuclear receptor co-repressor 1 Hydroxysteroids Cell Nucleus Chemistry Adenine Nucleotides Binding protein Prostate Dihydrotestosterone DNA Guanine Nucleotides Rats Models Structural Cytosol Nuclear receptor coactivator 3 Androgens Carrier Proteins Protein Binding |
| Zdroj: | Journal of steroid biochemistry. 3(3) |
| ISSN: | 0022-4731 |
| Popis: | 5α-Dihydrotestosterone can bind to specific receptor protein(s) in the microsomal or cytosol fractions of rat ventral prostate. The binding is highly steroid specific and correlated with the androgenicity of the steroids. A large part of the androgen molecule appears to be physically enveloped by the receptor protein molecule. Since certain derivatives of 17β-hydroxy-estra-4-ens also bind to the receptor protein, the detailed atomic arrangements and local electronic structure do not seem to be as important as the gross solid-geometric structure of an androgen for its ability to bind to the receptor molecule. A prior interaction and binding of 5α-dihydrotestosterone to the cytoplasmic receptor protein is required for the retention of the latter by cell nuclei of prostate. The nuclear retention of the cytoplasmic protein-5α-dihydrotestosterone complex is dependent on a heat-labile protein (nuclear acceptor) in the nuclei. The acceptor molecule is a nuclear acidic protein which appears to bind to double-stranded DNA, poly G or poly A and to a much lesser extent to poly U, poly C or heat-denatured DNA. Some possible biological implications of these studies are presented. |
| Databáze: | OpenAIRE |
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