Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation.

Abstract

The amino-terminal laminin G-like domain of human sex hormone-binding globulin (SHBG) contains a single high affinity steroid-binding site. Crystal structures of this domain in complex with several different steroid ligands have revealed that estradiol occupies the SHBG steroid-binding site in an opposite orientation when compared with 5 alpha… (More)

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