title: Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron.
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.
authors.affiliation: Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, Canada.
authors.forename: A H
authors.initials: AH
authors.lastname: Yang
authors.forename: R T
authors.initials: RT
authors.lastname: MacGillivray
authors.forename: J
authors.initials: J
authors.lastname: Chen
authors.forename: Y
authors.initials: Y
authors.lastname: Luo
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: G D
authors.initials: GD
authors.lastname: Brayer
authors.forename: A B
authors.initials: AB
authors.lastname: Mason
authors.forename: R C
authors.initials: RC
authors.lastname: Woodworth
authors.forename: M E
authors.initials: ME
authors.lastname: Murphy
mesh_terms: D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D006801:Humans; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D017354:Point Mutation; D011485:Protein Binding; D014168:Transferrin / Q000737:chemistry*
chemical_list: D014168:Transferrin; D007501:Iron