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

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

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 mut...

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Veröffentlicht in:Protein science 2000-01, Vol.9 (1), p.49-52
Hauptverfasser: YANG, AMY H.-W., MacGILLIVRAY, ROSS T.A., CHEN, JIE, LUO, YAOGUANG, WANG, YILI, BRAYER, GARY D., MASON, ANNE B., WOODWORTH, ROBERT C., MURPHY, MICHAEL E.P.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Substitution
crystal structure
Crystallography, X-Ray
human transferrin
Humans
iron
Iron - chemistry
Models, Molecular
mutant
Point Mutation
Protein Binding
Transferrin - chemistry
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Zusammenfassung: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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.9.1.49