Molecular structure of serum transferrin at 3.3-.ANG. resolution

Bailey, Susan; Evans, Robert W.; Garratt, Richard Charles; Gorinsky, B.; Hasnain, S.S.; Horsburgh, Christopher; Jhoti, Harren; Lindley, P. F.; Mydin, Assanah

doi:10.1021/bi00415a061

Cited by 391 publications

(271 citation statements)

References 52 publications

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“…The last co-ordination position of iron is occupied by a water molecule or a hydroxyl ion. Identical results have been obtained with rabbit serum transferrin and human lactoferrin [15,16]. Recent M6ssbauer studies have also confirmed the similarity between the two ironbinding sites in human transferrin [17].…”

Section: Transferrin and The Transferrin Receptorsupporting

confidence: 69%

The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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INTRODUCTIONThe role of transferrin and its cell surface receptor in cellular iron metabolism has received considerable interest during the last decade. Hence, over this period several reviews covering various aspects of the topic have been published.In this review we attempt to summarize the new knowledge and controversies encountered during the last 4-5 years. The focus is on iron metabolism by the hepatocyte. We also view the concept of transferrin-cell interactions from angles which previously may not have been given particular attention, and we include some aspects of iron metabolism not normally covered by reviews of this type. Central parts of what may be regarded as well-established knowledge either have been entirely omitted, or are only briefly described or mentioned to the extent considered relevant to the particular topic discussed. Important aspects of iron metabolism such as iron adsorption, haemochromatosis, ferritin iron and iron in infection and neoplasia are not covered in the present paper. Instead, the reader is referred to one or more of the recently published reviews [1-5] and references therein.

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Section: Transferrin and The Transferrin Receptorsupporting

confidence: 69%

The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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“…The molecule shows a very high sequence identity to the sequence of rabbit serum Tf, whose structure has been solved by X-ray crystallography (Bailey et al, 1988). We are building a partial model of human Tf based on the rabbit structure, but it remains to be seen whether this will allow us to reconstruct the antibody/Tf complex structure.…”

Section: Discussionmentioning

confidence: 99%

Cloning, characterization, and modeling of a monoclonal anti‐human transferrin antibody that competes with the transferrin receptor

Orlandini¹,

Santucci²,

Tramontano³

et al. 1994

Protein Science

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In this report we describe the isolation and characterization of a monoclonal antibody against human serum transferrin (Tf) and the cloning and sequencing of its cDNA. The antibody competes with the transferrin receptor (TR) for binding to human Tf and is therefore expected to bind at or very close to a region of interaction between Tf and its receptor. From the deduced amino acid sequence, we constructed a 3-dimensional model of the variable domains of the antibody based on the canonical structure model for the hypervariable loops. The proposed structure of the antibody is a first step toward a more detailed characterization of the antibody-Tf complex and possibly toward a better understanding of the Tf interaction with its receptor. The model might prove useful in guiding site-directed mutagenesis studies, simplifying the experimental elucidation of the antibody structure, and in the use of automatic procedures to dock the interacting molecules as soon as structural information about the structure of the human Tf molecule will be available.

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“…The cleft is formed by two domains, N-I and N-II in the N-lobe and C-I and C-II in the Clobe. In human lactoferrin (hLF), human serum transferrin (hTF), rabbit serum transferrin (rTF) and chicken ovotransferrin (oTF), crystallographic data show that each ferric ion is directly coordinated to the side chains of two tyrosine residues, one histidine residue, one aspartic acid residue and two oxygens from the synergistic carbonate anion [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Mutagenesis of the aspartic acid ligands in human serum transferrin: lobe–lobe interaction and conformation as revealed by antibody, receptor-binding and iron-release studies

Mason

Tam

et al. 1998

Biochemical Journal

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Recombinant non-glycosylated human serum transferrin and mutants in which the liganding aspartic acid (D) in one or both lobes was changed to a serine residue (S) were produced in a mammalian cell system and purified from the tissue culture media. Significant downfield shifts of 20, 30, and 45 nm in the absorption maxima were found for the D63S-hTF, D392S-hTF and the double mutant, D63S/D392S-hTF when compared to wild-type hTF. A monoclonal antibody to a sequential epitope in the C-lobe of hTF reported affinity differences between the apo- and iron-forms of each mutant and the control. Cell-binding studies performed under the same buffer conditions used for the antibody work clearly showed that the mutated lobe(s) had an open cleft. It is not clear whether the receptor itself may play a role in promoting the open conformation or whether the iron remains in the cleft.

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Molecular structure of serum transferrin at 3.3-.ANG. resolution

Cited by 391 publications

References 52 publications

The role of transferrin in the mechanism of cellular iron uptake

The role of transferrin in the mechanism of cellular iron uptake

Cloning, characterization, and modeling of a monoclonal anti‐human transferrin antibody that competes with the transferrin receptor

Mutagenesis of the aspartic acid ligands in human serum transferrin: lobe–lobe interaction and conformation as revealed by antibody, receptor-binding and iron-release studies

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