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| **[[3qyt]], [[3v83]], [[4x1b]] – hTF + Fe+3 - human<br /> | | **[[3qyt]], [[3v83]], [[4x1b]] – hTF + Fe+3 - human<br /> |
| **[[4x1d]] – hTF + Yb+3 <br /> | | **[[4x1d]] – hTF + Yb+3 <br /> |
| | **[[5dyh]] – hTF + Ti+4 <br /> |
| **[[4h0w]] – hTF + Fe+3 + Bi+3<br /> | | **[[4h0w]] – hTF + Fe+3 + Bi+3<br /> |
| **[[1suv]] – hTF + TF receptor <br /> | | **[[1suv]] – hTF + TF receptor <br /> |
Revision as of 08:30, 21 September 2016
| 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 two lobes: 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].
- ↑ 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
- ↑ 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
- ↑ 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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3D Structures of Transferrin
Updated on 21-September-2016
{"openlevels":0}
- Transferrin
- Transferrin N lobe
- 1tfd – rTF N terminal
- 1a8e, 1a8f, 1b3e, 1n84 - hTF N terminal
- 1dtg, 1d3k, 1d4n, 1fqe, 1fqf, 1jqf, 1n7w, 1n7x, 1oqg, 1oqh, 2o7u, 2o84, 3fgs - hTF N terminal (mutant)
- 1ryo - hTF N terminal + oxalate
- Transferrin C lobe
- Apo transferrin
- Ovotransferrin
- Ovotransferrin N lobe
- Apo ovotransferrin
References
