Transferrin

From Proteopedia

spinqualitylabelsall models Glycosylated human transferrin with Fe+3 (light red), carbonate and sulfate (PDB code 3qyt). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D Structures of Transferrin 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]. . . 3D Structures of Transferrin Transferrin 3D structures

References

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