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Protein Science, Vol 9, Issue 1 49-52, Copyright © 2000 by The Protein Society

JOURNAL ARTICLE

Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron

AH Yang, RT MacGillivray, J Chen, Y Luo, Y Wang, GD Brayer, AB Mason, RC Woodworth and ME Murphy
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, Canada.

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.
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