Article
Mutations at nonliganding residues Tyr-85 and Glu-83 in the N-lobe of human serum transferrin. Functional second shell effects.
The Journal of biological chemistry - 3 Jul 1998
He Q Y, Mason A B, Woodworth R C, Tam B M, MacGillivray R T, Grady J K, Chasteen N D
Abstract excerpt
The x-ray crystal structure of the N-lobe of human serum transferrin has shown that there is a hydrogen bond network, the so-called "second shell," around the transferrin iron binding site. Tyrosine at position 85 and glutamic acid at position 83 are two nonliganding residues in this network in the human serum transferrin N-lobe (hTF/2N). Mutation of each of these two amino acids has a profound effect on the...
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