Isolation and characterization of human TR3 receptor: a member of steroid receptor superfamily
- PMID: 2626032
- DOI: 10.1016/0022-4731(89)90114-3
Isolation and characterization of human TR3 receptor: a member of steroid receptor superfamily
Abstract
Complementary DNAs (cDNAs) encoding a member of steroid receptor super-family, named TR3 receptor, were isolated from a human prostate lambda gt11 cDNA library on the basis of homology of oligonucleotide probes to the DNA-binding domain common to members of the steroid receptor super-family. Expression of TR3 receptor cDNA produced a 64 kDa DNA-binding protein in a rabbit reticulocyte lysate. Nucleotide sequence analysis showed that TR3 receptor cDNA contains two regions of sequences which correspond to the DNA- and hormone-binding domains of members of the steroid receptor super-family. The amino acid sequences in the hormone-binding domain of the TR3 receptor shares about 20% homology with estrogen receptor and less than 15% homology with other known steroid receptors. The DNA-binding domain of the TR3 receptor has about 55% homology with all other known steroid receptors. TR3 receptor had 86% nucleotide and 91% amino acid sequence homology with mouse NUR/77, suggesting that TR3 receptor may be a human homologue of mouse NUR/77 gene product.
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