Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation.
Authors Grishkovskaya Irina; Avvakumov George V; Hammond Geoffrey L; Catalano Maria G; Muller Yves A;
JournalJ Biol Chem
PubMed ID12065592
'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-dihydrotestosterone or C19 ... More
Stable production of a human growth hormone antagonist from CHO cells adapted to serum-free suspension culture.
Authors Haldankar R; Kopchick J J; Ridgway D;
JournalBiotechnol Prog
PubMed ID10356250
Human growth hormone (hGH) is a polypeptide with 191 amino acids and a molecular mass of 22 kDa. An hGH analogue was created with a single amino acid substitution (glycine[G] 120 to arginine[R]) in the third alpha-helix of the hGH molecule. This hGH analogue, named hGHG120R, was found to be ... More
Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity.
Authors Grossmann M; Szkudlinski M W; Tropea J E; Bishop L A; Thotakura N R; Schofield P R; Weintraub B D;
JournalJ Biol Chem
PubMed ID7493973
We used a novel approach to study the role of the Asn-linked oligosaccharides for human thyrotropin (hTSH) activity. Mutagenesis of Asn (N) within individual glycosylation recognition sequences to Gln (Q) was combined with expression of wild type and mutant hTSH in cell lines with different glycosylation patterns. The in vitro ... More