The human estrogen receptor hormone binding domain dimerizes independently of ligand activation.
High level expression of biochemically active human estrogen receptor hormone binding domain (hER-HBD) was achieved using a Saccharomyces cerevisiae expression system. Using dissociation kinetic analysis, density gradient centrifugation and cross-linking studies, a spontaneous dimerization activity of hER-HBD independent of the presence of the DNA binding domain, ligand, and of elevated temperature is demonstrated.
Salomonsson
M
M
Karo Bio AB, Huddinge, Sweden.
Häggblad
J
J
O'Malley
B W
BW
Sitbon
G M
GM
D001665:Binding Sites; D002499:Centrifugation, Density Gradient; D003432:Cross-Linking Reagents; D003636:DEAE-Cellulose; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008567:Membranes, Artificial; D011108:Polymers; D011960:Receptors, Estrogen / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae
D003432:Cross-Linking Reagents; D004268:DNA-Binding Proteins; D008024:Ligands; D008567:Membranes, Artificial; D011108:Polymers; D011960:Receptors, Estrogen; D011994:Recombinant Proteins; D004958:Estradiol; D004247:DNA; D003636:DEAE-Cellulose