The preparation and partial characterization of <i>N</i>-terminal and <i>C</i>-terminal iron-binding fragments from rabbit serum transferrin

Heaphy, Shaun; Williams, Josh

doi:10.1042/bj2050611

Cited by 17 publications

(3 citation statements)

References 34 publications

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“…HST and human lactoferrin possess two glycan chains per molecule located at Asn437 and Asn611 for HST (MacGillivray et al, 1983) and at Asn137 and Asn490 for HLT (MetzBoutigue et al, 1984) in the N and C-lobes respectively. The carbohydrate content of RST is similar to that of the isolated C-lobe of ovotransferrin and consists of a single glycan chain (Heaphy & Williams, 1982;Evans, Aitken & Patel, 1988), and located at Asn491 (Bailey et al, 1988). This paper describes the determination of the crystal structure of diferric duck ovotransferrin at a resolution of 2.35 ,~.…”

Section: Duck Ovotransferrin Table 1 Secondary Structure In Duck Ovomentioning

confidence: 99%

“…A number of surface loops are ill defined as is the peptide link between the N-and C-lobes. There is interpretable density for three carbohydrate moieties of a single glycan chain on the DOT structure at Asn473; this is the equivalent residue to that glycosylated in HOT (Heaphy & Williams, 1982). An N-acetylglucosmaine (NAG) moiety is covalently linked through C3 to the ND2 of Asn473 at the C-terminal end of helix 5 (Table 1) in the C-lobe.…”

Section: Fold Of the Polypeptide Chainmentioning

confidence: 99%

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Structure of Diferric Duck Ovotransferrin at 2.35 Å Resolution

Rawas

Muirhead²,

Williams³

1996

Acta Cryst D

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The structure of diferric duck ovotransferrin (DOT) has been determined and refined at a resolution of 2.35 A. The DOT structure, which contains two iron binding sites, is similar to the known transferrin and lactoferrin structures. The two iron-binding sites, one in the Nterminal lobe and one in the C-terminal lobe of the molecule, are similar but not identical. The main differences between the three known structures lie in the relative orientations of the N-and C-lobes with respect to each other. In the DOT structure the large aromatic side chain of Phe322 in the N-lobe packs against the conserved residue Gly387 in the C-lobe. This interaction is at the centre of the interface between the two lobes and could play a crucial role in determining their relative orientation. Other differences between the structures occur in the surface loops and in the peptide connecting the two lobes. The final crystallographic model consists of 5309 protein atoms (686 residues), two Fe 3+ ions, two (bi)carbonate ions and three carbohydrate moities. 318 water molecules have been added to the model. The final R factor is 0.22 for 25400 observed reflections between 10 and 2.35A resolution. I. AbbreviationsDOT, duck ovotransferrin; HOT, hen ovotransferrin; HST, human serum transferrin; HMT, human melanotransferrin; RST, rabbit serum transferrin; HLT, human lactoferrin; MLT, mouse lactoferrin; MST, Manduca sexta transferrin; r.m.s., root-mean-square; NAG, N-acetylglucosamine; FUC, fucose.

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Section: Duck Ovotransferrin Table 1 Secondary Structure In Duck Ovomentioning

confidence: 99%

Section: Fold Of the Polypeptide Chainmentioning

confidence: 99%

Structure of Diferric Duck Ovotransferrin at 2.35 Å Resolution

Rawas

Muirhead²,

Williams³

1996

Acta Cryst D

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“…Des études cristallographiques de la protéine ont permis de visualiser deux domaines fonctionnels homologues : l'un N-terminal (résidus 1-336) et l'autre C-terminal (337-679) [12]. Il existe environ 50 % d'homologie entre les résidus d'acides aminés qui composent ces deux domaines [13]. Chacun des domaines peut fixer un ion Fe 3+ avec une très forte constante d'affinité comprise entre 1 à 6,10 -22 M -1 [14].…”

Section: Transferrineunclassified

A new function for transferrin expressed in testes

Fumel

Sow²,

Fouchécourt

et al. 2009

Basic Clin. Androl.

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Chez l'homme, les oligospermies sévères sont associées à un faible taux de transferrine dans le liquide séminal. La transferrine apparaît comme un bon indicateur pour définir les dysfonctionnements testiculaires. Son niveau d'expression dans le testicule doit être parfaitement contrôlé. Elle y joue un rôle dans le transport du fer. Mais de récents résultats montrent l'existence d'une forme dimérique de la transferrine sertolienne comme puissant régulateur de la phagocytose des corps résiduels par les cellules de Sertoli. Mots clés Transferrine · Testicule · Cellules de Sertoli · Phagocytose · Corps résiduelAbstract In men, oligozoospermia corresponds with a low level of transferrin in semen. Transferrin appears to be a relevant indicator of gonadal function. Transferrin expression in normal testes is perfectly controlled. Transferrin contributes to iron transport. However, recent results show the existence of a dimeric form, which acts as a powerful regulator of phagocytosis of residual bodies by Sertoli cells. A disturbance of this new highlighted function may account for some forms of oligozoospermia.

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Transferrins

Brock¹

1985

Metalloproteins

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The preparation and partial characterization of N-terminal and C-terminal iron-binding fragments from rabbit serum transferrin

Cited by 17 publications

References 34 publications

Structure of Diferric Duck Ovotransferrin at 2.35 Å Resolution

Structure of Diferric Duck Ovotransferrin at 2.35 Å Resolution

A new function for transferrin expressed in testes

Transferrins

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