The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural study (Q27640054)

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15 December 2019

title

The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural study (English)

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3

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author name string

Ty E Adams

1

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15 December 2019

Anne B Mason

2

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15 December 2019

Peter J Halbrooks

4

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15 December 2019

Sara K Briggs

5

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15 December 2019

Valerie C Smith

6

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Ross T A MacGillivray

7

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Stephen J Everse

8

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language of work or name

English

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publication date

27 November 2002

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Journal of Biological Chemistry

15 December 2019

published in

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volume

278

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issue

8

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page(s)

6027-6033

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Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants

15 December 2019

cites work

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Anion-mediated iron release from transferrins. The kinetic and mechanistic model for N-lobe of ovotransferrin.

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Chemistry and biology of eukaryotic iron metabolism

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pH and the recycling of transferrin during receptor-mediated endocytosis

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Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release

21 January 2018

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

21 January 2018

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Crystal structure and iron-binding properties of the R210K mutant of the N-lobe of human lactoferrin: implications for iron release from transferrins

21 January 2018

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The chloride effect is related to anion binding in determining the rate of iron release from the human transferrin N-lobe

21 January 2018

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

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Lactoferrin and transferrin: functional variations on a common structural framework

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Crystal structure of diferric hen ovotransferrin at 2.4 A resolution

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A general method of site-specific mutagenesis using a modification of the Thermus aquaticus polymerase chain reaction

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron-release trigger and anion-binding site

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The synergistic anion-binding sites of human transferrin: chemical and physiological effects of site-directed mutagenesis

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Transferrins: iron release from lactoferrin.

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Transferrins, the mechanism of iron release by ovotransferrin.

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Studies on the mechanism of iron release from transferrin

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The evolution of transferrin

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Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe

21 January 2018

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The mechanism of iron release from transferrin. Slow-proton-transfer-induced loss of nitrilotriacetatoiron(III) complex in acidic media

21 January 2018

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Release of iron from C-terminal monoferric transferrin to phosphate and pyrophosphate at pH 5.5 proceeds through two pathways

21 January 2018

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A kinetically active site in the C-lobe of human transferrin

21 January 2018

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Iron Release from Recombinant N-lobe and Mutants of Human Transferrin

21 January 2018

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Efficient production and isolation of recombinant amino-terminal half-molecule of human serum transferrin from baby hamster kidney cells

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M210349200

1 reference

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15 December 2019

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