Transferrins

Brock, Jeremy H.

doi:10.1007/978-1-349-06375-8_5

Cited by 99 publications

(83 citation statements)

References 539 publications

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“…Both the N and the C lobes contain about 330 amino acids and are made up of two domains N1, N2 and C 1, C2 respectively, with the iron binding site situated in the interdomain cleft. Diferric transferrins have the ability to bind two Fe 3÷ ions concomitantly with two carbonate CO~-anions (Brock, 1985;Crichton, 1991). The crystallographic structure determinations of human lactoferrin (Anderson et al, 1987;Anderson, Baker, Noms, Rice & Baker, 1989), rabbit serum transfemn (Bailey et al, 1988), the N-terminal half molecule of RST (Sarra, Garratt, Gorinsky, Jhoti & Lindley, 1990), the N-terminal half-molecule of hen ovotransferrin (Dewan, Mikami, Hirose & Sacchettini, 1993), HOT (Kurokawa, Mikami & Hirose, 1995), the mutant Asp60Ser of the N-terminal half-molecule of HLT (Faber et al, 1996) and duck ovotransferrin (Rawas, Muirhead & Williams, 1996) have provided structural information regarding the organization of these proteins in the presence of iron, the environment of the iron binding sites, and the interdomain interactions.…”

Section: Introductionmentioning

confidence: 99%

Structure of apo duck ovotransferrin: the structures of the N and C lobes are in the open form

Rawas

Muirhead²,

Williams³

1997

Acta Cryst D

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The structure of apo duck ovotransfemn (APODOT) has been determined at a resolution of 4.0A by the molecular replacement method using the structure of duck ovotransfemn (DOT) as the search model. The DOT structure contains two iron binding sites; one in the N-terminal lobe lying between domains N1 and N2 and one in the C-terminal lobe between domains C 1 and C2. Both lobes have a closed structure. Models of various forms of both the N and C lobes were used in the search. The final model was refined to give an R factor of 0.22. The comparison of the structure of APODOT with that of DOT shows that both the N and the C lobes are in an open form, where the N2 and C2 domains undergo large rigid-body rotations of 51.6 and 49.9 ° relative to the N1 and C1 domains, respectively. The interface between the N and C lobes, which is formed by the N1--C 1 contact in the core of the molecule does not change significantly. The DOT molecule may be described in terms of three rigid bodies; the N1 and C1 domains as one rigid body forming the static core of the molecule and the N2 and C2 domains as two other rigid bodies which, on the release of iron, move away from the static core of the molecule to form the open structure of APODOT.

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Section: Introductionmentioning

confidence: 99%

Structure of apo duck ovotransferrin: the structures of the N and C lobes are in the open form

Rawas

Muirhead²,

Williams³

1997

Acta Cryst D

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“…Lactoferrin is a member of the transferrin family of iron-binding proteins, which also includes serum transferrin and ovotransferrin (Aisen & Listowsky, 1980;Brock, 1985). These monomeric glycoproteins, of molecular weight -80 000 dalton, have specific binding sites for two Fe 3 + ions together with two CO32 ions per molecule.…”

Section: Introductionmentioning

confidence: 99%

Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change

Norris

Anderson²,

Baker³

1991

Acta Crystallogr Sect B

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The crystal structure of an orthorhombic form of human apolactoferrin (ApoLf) has been determined from 2.8 ~ diffractometer data by molecular replacement methods. A variety of search models derived from the diferric lactoferrin structure (Fe2Lf) were used to obtain a consistent solution to the rotation function. An R-factor search gave the correct translational solution and the model was refined by rigid-body least-squares refinement (program CORELS). Only three of the four domains were located correctly by this procedure, however; the fourth was finally placed correctly by rotating it manually onto three strands of electron density which were recognized as part of its central/3-sheet. The final model, refined by restrained least-squares methods to an R factor of 0.214 for data in the resolution range 10.0 to 2.8 A~, shows a large domain movement in the N-terminal half of the molecule (a 54 rotation of domain N2) and smaller domain movements elsewhere, when compared with Fe=Lf. A feature of the crystal structure is that although the ApoLf and Fe2Lf unit cells appear very similar, their crystal packing and molecular structures are quite different.

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“…Transferrin is a singlechain glycoprotein (80 kDa) present in blood at a concentration of about 35 M, and consists of two similar lobes, each of 40 kDa, connected by a short peptide. Its normal function in blood is to carry iron between sites of uptake, utilization, and storage (13)(14)(15)(16). It contains two specific iron-binding sites per molecule, one in the N-terminal lobe and one in the C-terminal lobe.…”

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confidence: 99%

“…Iron cannot bind strongly without concomitant binding of a synergistic anion. Since transferrin is only about 30% saturated with iron in normal serum (13,17,18), there is potential binding capacity for other metal ions that enter the blood. This has led to the idea that transferrin acts as a "delivery system" for therapeutic, diagnostic or toxic ions, including Ga 3ϩ , Ru 3ϩ , and Al 3ϩ (19 -21).…”

mentioning

confidence: 99%

“…It is therefore now important to establish whether Bi 3ϩ binding to transferrin can occur under physiologically relevant conditions, especially in the presence of excess albumin and in blood plasma itself. We have shown previously that the order of lobe loading of hTF with metal ions can readily be determined via two-dimensional 1 H, 13 C NMR studies of recombinant [⑀- 13 C]Met-hTF (23). It is known that the strength of binding to the two lobes is slightly different, and that Fe 3ϩ is primarily situated in N-lobe in serum (14,18).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Competitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma

Sun

Mason

et al. 2001

Journal of Biological Chemistry

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Transferrins

Cited by 99 publications

References 539 publications

Structure of apo duck ovotransferrin: the structures of the N and C lobes are in the open form

Structure of apo duck ovotransferrin: the structures of the N and C lobes are in the open form

Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change

Competitive Binding of Bismuth to Transferrin and Albumin in Aqueous Solution and in Blood Plasma

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