Function

Transferrin or serotransferrin (TF) is an iron-binding protein. TF delivers iron from absorption centers in the duodendum and white blood cell macrophages to all tissues[1]. Ovotransferrin (OTF) is a glycosylated TF of egg white. For details see Molecular Playground/Transferrin.

Relevance

Carbohydrate-deficient TF may help diagnose alcoholic liver disease[2].

Structural highlights

TF contains : at the N and C termini. The Fe+3 ion is coordinated to several side chains belonging to both N- and C-lobe, carbonate and sulfate ions[3].

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3D Structures of Transferrin

Transferrin 3D structures


Glycosylated human transferrin with Fe+3 (light red), carbonate and sulfate (PDB code 3qyt).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. de Jong G, van Dijk JP, van Eijk HG. The biology of transferrin. Clin Chim Acta. 1990 Sep;190(1-2):1-46. PMID:2208733
  2. Liu YS, Xu GY, Cheng DQ, Li YM. Determination of serum carbohydrate-deficient transferrin in the diagnosis of alcoholic liver disease. Hepatobiliary Pancreat Dis Int. 2005 May;4(2):265-8. PMID:15908327
  3. Yang N, Zhang H, Wang M, Hao Q, Sun H. Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe. Sci Rep. 2012;2:999. doi: 10.1038/srep00999. Epub 2012 Dec 19. PMID:23256035 doi:10.1038/srep00999

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