Literature DB >> 10739246

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

A H Yang1, R T MacGillivray, J Chen, Y Luo, Y Wang, G D Brayer, A B Mason, R C Woodworth, M E Murphy.   

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.

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Year:  2000        PMID： 10739246      PMCID： PMC2144434          DOI： 10.1110/ps.9.1.49

Source DB:  PubMed          Journal:  Protein Sci        ISSN： 0961-8368            Impact factor:   6.725


  23 in total

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Authors:  Y Wang; J Chen; Y Luo; W D Funk; A B Mason; R C Woodworth; R T MacGillivray; G D Brayer
Journal:  J Mol Biol       Date:  1992-09-20       Impact factor: 5.469

2.  Molecular structure of serum transferrin at 3.3-A resolution.

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Journal:  Biochemistry       Date:  1988-07-26       Impact factor: 3.162

Review 3.  Transferrin, the transferrin receptor, and the uptake of iron by cells.

Authors:  P Aisen
Journal:  Met Ions Biol Syst       Date:  1998

4.  X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.

Authors:  M C Bewley; B M Tam; J Grewal; S He; S Shewry; M E Murphy; A B Mason; R C Woodworth; E N Baker; R T MacGillivray
Journal:  Biochemistry       Date:  1999-02-23       Impact factor: 3.162

5.  Production and isolation of the recombinant N-lobe of human serum transferrin from the methylotrophic yeast Pichia pastoris.

Authors:  A B Mason; R C Woodworth; R W Oliver; B N Green; L N Lin; J F Brandts; B M Tam; A Maxwell; R T MacGillivray
Journal:  Protein Expr Purif       Date:  1996-08       Impact factor: 1.650

6.  Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin.

Authors:  R C Woodworth; A B Mason; W D Funk; R T MacGillivray
Journal:  Biochemistry       Date:  1991-11-12       Impact factor: 3.162

7.  Calorimetric studies of the N-terminal half-molecule of transferrin and mutant forms modified near the Fe(3+)-binding site.

Authors:  L N Lin; A B Mason; R C Woodworth; J F Brandts
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8.  Mutations at nonliganding residues Tyr-85 and Glu-83 in the N-lobe of human serum transferrin. Functional second shell effects.

Authors:  Q Y He; A B Mason; R C Woodworth; B M Tam; R T MacGillivray; J K Grady; N D Chasteen
Journal:  J Biol Chem       Date:  1998-07-03       Impact factor: 5.157

9.  Kinetic studies on the removal of iron and aluminum from recombinant and site-directed mutant N-lobe half transferrins.

Authors:  Y Li; W R Harris; A Maxwell; R T MacGillivray; T Brown
Journal:  Biochemistry       Date:  1998-10-06       Impact factor: 3.162

10.  Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.

Authors:  P D Jeffrey; M C Bewley; R T MacGillivray; A B Mason; R C Woodworth; E N Baker
Journal:  Biochemistry       Date:  1998-10-06       Impact factor: 3.162
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2.  A mechanistic examination of salting out in protein-polymer membrane interactions.

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3.  A computational study of the open and closed forms of the N-lobe human serum transferrin apoprotein.

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Journal:  Biophys J       Date:  2003-12       Impact factor: 4.033

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Journal:  Nat Commun       Date:  2022-09-14       Impact factor: 17.694

7.  Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies.

Authors:  Claudia G Chilom; Nicoleta Sandu; Sorina Iftimie; Maria Bălăşoiu; Andrey Rogachev; Oleg Orelovich; Sergey Stolyar
Journal:  Int J Mol Sci       Date:  2021-06-29       Impact factor: 5.923
  7 in total

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