Metal-induced conformational changes in transferrins.
Recent studies on iron-loaded transferrins have revealed a conformational change upon binding iron due to a domain closure. It has been suggested that the domain closure may be the key for the receptor recognition of the metal loaded transferrin (Grossmann et al., 1992). Small angle X-ray scattering has been used to provide direct structural information on the conformational changes that may take place upon the binding and release of different metals to the transferrins in solution. The data show that In3+ and Cu2+ induce the same domain closure as Fe3+; Al3+ causes a conformational change of somewhat smaller magnitude while Hf4+ does not induce any conformational change. The results are discussed in terms of the molecular recognition of metal loaded transferrin by the receptor.
Grossmann
J G
JG
Molecular Biophysics Group, SERC Daresbury Laboratory, Warrington, Cheshire, U.K.
Neu
M
M
Evans
R W
RW
Lindley
P F
PF
Appel
H
H
Hasnain
S S
SS
D008670:Metals / Q000737:chemistry*; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D014168:Transferrin / Q000737:chemistry*
D008670:Metals; D012996:Solutions; D014168:Transferrin