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- W2006608757 abstract "The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris. The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 Å resolution. This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin. The polypeptide folding pattern is essentially identical in all of the three proteins. Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose. This represents the first localization of an O-linked glycan in a P. pastoris-derived protein. Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N." @default.
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- W2006608757 date "1999-02-01" @default.
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- W2006608757 title "X-ray Crystallography and Mass Spectroscopy Reveal that the N-lobe of Human Transferrin Expressed in <i>Pichia pastoris</i> Is Folded Correctly but Is Glycosylated on Serine-32<sup>,</sup>" @default.
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- W2006608757 doi "https://doi.org/10.1021/bi9824543" @default.
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