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 t...
Topics
- Base Sequence
- Copper
- DNA Primers
- Electron Spin Resonance Spectroscopy
- Glutamic Acid
- Humans
- Hydrogen Bonding
- Iron
- Ligands
- Mutation
- Protein Binding
- Transferrin
- Tyrosine