1998
DOI: 10.1021/bi980318s
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Iron Release Is Reduced by Mutations of Lysines 206 and 296 in Recombinant N-Terminal Half-Transferrin

Abstract: Human serum transferrin consists of two iron-binding lobes connected by a short peptide linker. While the high homology and structural similarity between the two halves of the molecule would suggest similar characteristics, it has been shown that the pH-dependent rate of release of iron from the N-terminal lobe is quite different from that of its C-terminal counterpart. This suggests that the N-lobe of human serum transferrin has a specific, pH-dependent, molecular mechanism for releasing iron. Sacchettini and… Show more

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Cited by 35 publications
(40 citation statements)
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“…Recombinant transferrin has been successfully produced using both prokaryotic [19e21] and eukaryotic [22,23] expression systems. These studies used recombinant transferrin to further characterize its iron-binding properties [24], to study the interactions of transferrin with pathogen receptors [25], and to develop approaches for the biological delivery of peptide drugs [26]. To our knowledge, the role of recombinant transferrin as a modulator of immune responses has not been reported previously.…”
Section: Discussionmentioning
confidence: 99%
“…Recombinant transferrin has been successfully produced using both prokaryotic [19e21] and eukaryotic [22,23] expression systems. These studies used recombinant transferrin to further characterize its iron-binding properties [24], to study the interactions of transferrin with pathogen receptors [25], and to develop approaches for the biological delivery of peptide drugs [26]. To our knowledge, the role of recombinant transferrin as a modulator of immune responses has not been reported previously.…”
Section: Discussionmentioning
confidence: 99%
“…Previous works have shown that the N and C-lobes from Tf contain pH-sensitive residues monitoring the conformational changes of Tf: The di-lysine motif 14 Lys206/Lys296 in N-lobe, the Lys534/Arg632/Asp634 triad 15 and the His349/Lys511 motif 16 within the C-lobe. Within the TbpB–hTf structure the His349/Lys511 motif in hTf is buried in the binding interface, and the His349 residue interacts with TbpB through a bridging tetra-coordinated water H-bonded to Asp159, His143, Lys206 from TbpB and His349 from hTf (Figure 2 and Supplementary Figure 2D–H).…”
mentioning
confidence: 99%
“…The P. pastoris KM71 (HIS4 Ϫ , AOX1 Ϫ ) strain was transformed by electroporation, and positive transformants were selected on zeocin-containing YPDS (1% yeast extract, 2% peptone, 2% dextrose, 1 M sorbitol, 100 g/ml zeocin) plates as described in the Pichia Expression System users manual (Invitrogen). Zeocin-resistant colonies were screened for protein expression in small volume cultures according to a procedure described previously (23).…”
Section: Cloning the Frz Domain Of Rat Ror1mentioning
confidence: 99%