The effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study.
Distance distribution functions, p(r), radii of gyration, Rg, and radii of gyration of cross section, Rq, of apotransferrin, monoferric transferrin, and diferric transferrin have been compared. The alteration of Rg and Rq upon iron binding has been determined by a difference method. An unusual feature of the stepwise structural changes of transferrin upon iron saturation is that binding of the first ferric ion is responsible for more than half of the whole change in Rq, whereas Rg alters significantly only after the binding of the second ferric ion.
D006801:Humans; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D011485:Protein Binding; D011487:Protein Conformation; D012542:Scattering, Radiation; D014168:Transferrin / Q000378:metabolism*; D014965:X-Rays
D014168:Transferrin; D007501:Iron