Cysteine-10 on 17β-Hydroxysteroid Dehydrogenase 1 Has Stabilizing Interactions in the Cofactor Binding Region and Renders Sensitivity to Sulfhydryl Modifying Chemicals
Figure 1
Sequence alignment of the cofactor binding domain of 17β-HSD1. Peptide sequences of human (h), bovine (bt), rat (rn), mouse (mm), and zebrafish (Danio rerio, dr) 17β-HSD1 (SDR28C1) are shown in the upper panel and those of the related human SDR enzymes all-trans retinol dehydrogenase RDH8 (SDR28C2), hydroxybutyrate dehydrogenase BDH (SDR9C1), 17β-HSD2 (SDR9C2), 11β-HSD2 (SDR9C3), 3α-HSD (SDR9C4), 11-cis retinol dehydrogenase (SDR9C5), 17β-HSD6 (SDR9C6), retinol dehydrogenase SDR-O (SDR9C7), and retinol dehydrogenase RDH16 (SDR9C8) in the lower panel. The locations of β-strand A through β-strand B are indicated above the alignment. The position of the conserved Cys10 on 17β-HSD1 is indicated by an arrow and the conserved glycine residues of the Rossmann-fold by asterisks (in bold).
