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Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron

Published online by Cambridge University Press:  01 January 2000

AMY H.-W. YANG ,
ROSS T.A. MacGILLIVRAY ,
JIE CHEN ,
YAOGUANG LUO ,
YILI WANG ,
GARY D. BRAYER ,
ANNE B. MASON ,
ROBERT C. WOODWORTH  and
MICHAEL E.P. MURPHY
AMY H.-W. YANG
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
ROSS T.A. MacGILLIVRAY
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
JIE CHEN
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
YAOGUANG LUO
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
YILI WANG
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
GARY D. BRAYER
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
ANNE B. MASON
Affiliation:
Department of Biochemistry, University of Vermont, Burlington, Vermont 05405-0068
ROBERT C. WOODWORTH
Affiliation:
Department of Biochemistry, University of Vermont, Burlington, Vermont 05405-0068
MICHAEL E.P. MURPHY
Affiliation:
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
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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

crystal structurehuman transferrinironmutant

Information

Type
Research Article
Information
Protein Science , Volume 9 , Issue 1 , January 2000 , pp. 49 - 52
Copyright
© 2000 The Protein Society

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