[HTML][HTML] Resolution of the human sex hormone-binding globulin dimer interface and evidence for two steroid-binding sites per homodimer
GV Avvakumov, I Grishkovskaya, YA Muller… - Journal of Biological …, 2001 - ASBMB
Human sex hormone-binding globulin (SHBG) transports sex steroids in the blood. It
functions as a homodimer, but there is little information about the topography of its
dimerization domain, and its steroid binding stoichiometry is controversial. The prevailing
assumption is that each homodimeric SHBG molecule contains a single steroid-binding site
at the dimer interface. However, crystallographic analysis of the amino-terminal laminin G-
like domain of human SHBG has shown that the dimerization and steroid-binding sites are …
functions as a homodimer, but there is little information about the topography of its
dimerization domain, and its steroid binding stoichiometry is controversial. The prevailing
assumption is that each homodimeric SHBG molecule contains a single steroid-binding site
at the dimer interface. However, crystallographic analysis of the amino-terminal laminin G-
like domain of human SHBG has shown that the dimerization and steroid-binding sites are …