In silico prediction
of the intrinsic disorder and ligand binding sites of human 3β-hydroxysteroid dehydrogenase
type 2 enzyme
Goswami Achintya Mohan
Res. J. Biotech.; Vol. 20(2); 140-146;
doi: https://doi.org/10.25303/202rjbt1400146; (2025)
Abstract
In human, the 3β-hydroxysteroid dehydrogenase (HSD3B)/Δ4,5-isomerase is an important
enzyme in steroid hormone biosynthesis. It catalyzed the conversion of Δ5-steroid
precursors to respective Δ4-ketosteroids. There were two HSD3B isoenzymes designated
as type 1(HSD3B1) and type 2 (HSD3B2), encoded by two different genes located in
chromosome 1p13.1. The mutations in HSD3B2 gene could lead to congenital adrenal
hyperplasia and impaired steroidogenesis in both the adrenals and gonads leading
to varieties of phenotypes. It was known that many proteins had intrinsically disordered
regions (IDRs) and sometimes the entire protein lacked a stable tertiary structure,
known as intrinsically disordered proteins (IDPs). These IDRs were attractive target
for potential drug discovery.
The HSD3B2 was found to possess several IDRs and the regions of IDRs varied according
to the algorithm or server used to predict them. The HSD3B2 was predicted to contain
two ligand binding sites for NAD and ATP and a single cavity. Some amino acid residues
involved in formation of cavity and ligand binding sites were within the intrinsically
disordered regions.
