Crystal Structures of Two Mutants (K206Q, H207E) of the N-lobe of Human Transferrin With Increased Affinity for Iron

Protein Sci. 2000 Jan;9(1):49-52. doi: 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 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Substitution
  • Crystallography, X-Ray
  • Humans
  • Iron / chemistry*
  • Models, Molecular
  • Point Mutation
  • Protein Binding
  • Transferrin / chemistry*

Substances

  • Transferrin
  • Iron