The cDNA‐deduced primary structure of human sex hormone‐binding globulin and location of its steroid‐binding domain

  title={The cDNA‐deduced primary structure of human sex hormone‐binding globulin and location of its steroid‐binding domain},
  author={Geoffrey L. Hammond and D Alan Underhill and C. L. Smith and Ing Swie Goping and M J Harley and Neal A. Musto and C. Yan Cheng and C. Wayne Bardin},
  journal={FEBS Letters},
The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs.
Southern blots of human placental DNA and cloned genomic DNA fragments indicate that sex hormone-binding globulin (SHBG) and its related testicular cDNAs are the products of a single gene.
Resolution of the steroid-binding and dimerization domains of human sex hormone-binding globulin by expression in Escherichia coli.
The data suggest that the N-terminal region of SHBG dimerizes readily in the absence of GST and in doing so acquires steroid-binding sites.
Mutagenesis of essential functional residues of rat androgen-binding protein/sex hormone-binding globulin.
Modifications of the ABP primary sequence throughout the molecule have a detrimental effect on steroid binding and secretion, and are demonstrated that at least part of active site is located in residues 139-150, but most of the protein is required to maintain the conformation of the active site.
Sex hormone-binding globulin/androgen-binding protein: Steroid-binding and dimerization domains
Selective removal of glycosylation sites from sex hormone-binding globulin by site-directed mutagenesis.
Site-directed mutagenesis of a human SHBG cDNA has enabled us to selectively disrupt the known glycosylation sites individually and in various combinations, and it was found that the presence of carbohydrates is not an absolute requirement for the secretion of SHBG from these cells, but the absence of both N-linked oligosaccharides reduced the amount of SH BG in the culture medium.
Analysis of the steroid binding domain of rat androgen-binding protein.
The site-directed photoaffinity ligand [3H]17 beta-hydroxy-4,6-androstadien-3-one (delta 6- testosterone) was used to label the steroid binding domain of rat androgen-binding protein (rABP) and several different amino acids appear to have been labeled as expected given the free radical nature of photoactivated delta 6-testosterone.
Hormonal regulation of rat androgen-binding protein (ABP) messenger ribonucleic acid and homology of human testosterone-estradiol-binding globulin and ABP complementary deoxyribonucleic acids.
Complementary DNA clones coding for rat androgen-binding protein (rABP) were isolated from a rat testis cDNA library constructed in the bacteriophage lambda gt11 and demonstrate that the cDNAs for human testosterone-estradiol binding globulin and human ABP have greater sequence similarity with each other than either has with rABP.
Structure-function relationships of rat androgen--binding protein/human sex-hormone binding globulin: the effect of mutagenesis on steroid-binding parameters.
It was found that recombinant wild-type rat ABP/SHBG bound DHT and estradiol with nearly the same affinities as human SHBG, rather than the affinITIES of rat epididymal ABP.
The gene structure of rat androgen-binding protein: identification of potential regulatory deoxyribonucleic acid elements of a follicle-stimulating hormone-regulated protein.
Southern blot analysis of rat genomic DNA indicated that there is a single gene for ABP in the rat, which supports the idea that sex hormone binding globulin produced by fetal rat liver is coded by the same gene.


Rat androgen-binding protein: evidence for identical subunits and amino acid sequence homology with human sex hormone-binding globulin.
The cDNA for rat androgen-binding protein (ABP) was previously isolated from a bacteriophage lambda gt11 rat testis cDNA library and its identity was confirmed by epitope selection. Hybrid-arrested
Amino acid sequence of the sex steroid binding protein of human blood plasma.
The amino acid sequence of the sex steroid binding protein (SBP) from human plasma has been determined and shows no homology either with the cDNA-derived sequences of the estrogen and glucocorticoid receptors found by others to be homologous with each other or with any other protein sequence in the 1986 data base.
Human testicular androgen-binding protein shares immunodeterminants with serum testosterone-estradiol-binding globulin.
HABP (peak I), peak II activity, and hTeBG have common immunodeterminants and it is concluded that if hABP is secreted into the blood of men, then its carbohydrate chains bind to Con A, making it indistinguishable from hTe BG under these conditions.