Inequivalent Contribution of the Five Tryptophan Residues in the C-Lobe of Human Serum Transferrin to the Fluorescence Increase when Iron is Released-Reference-Cited by-同舟云学术

Inequivalent Contribution of the Five Tryptophan Residues in the C-Lobe of Human Serum Transferrin to the Fluorescence Increase when Iron is Released

Published:2009-03-12 Issue:13 Volume:48 Page:2858-2867
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

James Nicholas G.¹,Byrne Shaina L.¹,Steere Ashley N.¹,Smith Valerie C.¹,MacGillivray Ross T. A.¹,Mason Anne B.¹

Affiliation:

1. Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Burlington, Vermont 05405, and Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8022834

Reference55 articles.

1. Human transferrin: cDNA characterization and chromosomal localization.

2. Ligand-Induced Conformational Change in Transferrins: Crystal Structure of the Open Form of the N-Terminal Half-Molecule of Human Transferrin,

3. Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal a Structural Change Implicated in Iron Release,

4. The Crystal Structure of Iron-free Human Serum Transferrin Provides Insight into Inter-lobe Communication and Receptor Binding

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