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human transferrin

Protein Science (1)

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Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron
AMY H.-W. YANG, ROSS T.A. MacGILLIVRAY, JIE CHEN, YAOGUANG LUO, YILI WANG, GARY D. BRAYER, ANNE B. MASON, ROBERT C. WOODWORTH, MICHAEL E.P. MURPHY
Journal:

Protein Science / Volume 9 / Issue 1 / January 2000

Published online by Cambridge University Press:

01 January 2000, pp. 49-52

Print publication:

January 2000
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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 Å, 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.