Crystal structures of two mutants (K206Q, H207E) of the N‐lobe of human transferrin with increased affinity for iron
- 1 January 2000
- journal article
- Published by Wiley in Protein Science
- Vol. 9 (1), 49-52
- https://doi.org/10.1110/ps.9.1.49
Abstract
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.Keywords
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