Conformational changes in the human estrogen receptor observed by (19)F NMR.
The (19)F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282-595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the empty receptor to have more conformational flexibility than the liganded form. This study shows the applicability of (19)F NMR to study conformational change in large protein systems.
Luck
L A
LA
Department of Chemistry and Biology, Clarkson University, Potsdam, New York 13699, USA. luckla@clarkson.edu
Barse
J L
JL
Luck
A M
AM
Peck
C H
CH
D001665:Binding Sites; D004958:Estradiol / Q000378:metabolism; D005461:Fluorine; D005982:Glutathione Transferase / Q000737:chemistry; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D011960:Receptors, Estrogen / Q000737:chemistry* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D014364:Tryptophan
D008024:Ligands; D011960:Receptors, Estrogen; D011993:Recombinant Fusion Proteins; D005461:Fluorine; D004958:Estradiol; D014364:Tryptophan; D005982:Glutathione Transferase