Journal article
Analysis of the Steroid Binding Domain of Rat Androgen-Binding Protein
Endocrinology (Philadelphia), Vol.129(2), pp.690-696
08/1991
Handle:
https://hdl.handle.net/2376/107334
PMID: 1855466
Abstract
The site-directed photoaffinity ligand [3H]17β-hydroxy-4,6-androstadien-3-one (δ6-testosterone) was used to label the steroid binding domain of rat androgen-binding protein (rABP). After digestion with trypsin, the major radiolabeled peptide was isolated by reverse phase chromatography. The peptide was found to have the following amino acid sequence: He Ala Leu Gly Gly Leu Leu Leu Pro Thr Ser. Gaps in the sequence that one would anticipate if δ6-testosterone formed an adduct with a single amino acid were not encountered. Several different amino acids appear to have been labeled as expected given the free radical nature of photoactivated δ6-testosterone.The sequence obtained corresponded to a tryptic peptide (amino acids 171–181) of the rABP precursor. The only other protein having this amino acid sequence was human sex hormone binding globulin. The binding domain lies in a hydrophobic pocket that contains a predicted β-sheet and turn secondary structure, as would be anticipated given the hydrophobic nature of the steroid molecule. A hydropathy and secondary structure analysis of rABP was performed as a basis for discussing the results of the current study in relation to previous studies on the steroid binding domain on human sex hormone binding globulin.
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Details
- Title
- Analysis of the Steroid Binding Domain of Rat Androgen-Binding Protein
- Creators
- BENJAMIN J DANZOJEFF A PARROTTMICHAEL K SKINNER
- Publication Details
- Endocrinology (Philadelphia), Vol.129(2), pp.690-696
- Academic Unit
- Biological Sciences, School of
- Identifiers
- 99900547507001842
- Language
- English
- Resource Type
- Journal article