Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron.
The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.
Yang
A H
AH
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, Canada.
MacGillivray
R T
RT
Chen
J
J
Luo
Y
Y
Wang
Y
Y
Brayer
G D
GD
Mason
A B
AB
Woodworth
R C
RC
Murphy
M E
ME
D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D006801:Humans; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D017354:Point Mutation; D011485:Protein Binding; D014168:Transferrin / Q000737:chemistry*
D014168:Transferrin; D007501:Iron