Isolation and characterization of human TR3 receptor: A member of steroid receptor superfamily

doi:10.1016/0022-4731(89)90114-3

Journal of Steroid Biochemistry

Volume 34, Issues 1–6, 1989, Pages 391-395

https://doi.org/10.1016/0022-4731(89)90114-3 Get rights and content

Abstract

Complementary DNAs (cDNAs) encoding a member of steroid receptor super-family, named TR3 receptor, were isolated from a human prostate λgt11 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 64kDa 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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^☆: Proceedings of the 9th International Symposium of the Journal of Steroid Biochemistry, Recent Advances in Steroid Biochemistry, Las Palmas, Canary Islands, Spain, 28–31 May 1989.

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Isolation and characterization of human TR3 receptor: A member of steroid receptor superfamily☆

Abstract

Cell

Biochem. biophys. Res. Commun.

Cell

Cell

Cell

J. steroid Biochem.

J. steroid Biochem.

Biochem. biophys. Res. Commun.