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Transferrin
From Proteopedia
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| - | <StructureSection load='' size=' | + | <StructureSection load='' size='350' side='right' caption='Glycosylated human transferrin with Fe+3 (light red), carbonate and sulfate (PDB code [[3qyt]]).' scene='48/480879/Cv/1' pspeed='8'> |
== Function == | == 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<ref>PMID:2208733</ref>. '''Ovotransferrin''' (OTF) is a glycosylated TF of egg white. For details see [[Molecular Playground/Transferrin]]. | '''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<ref>PMID:2208733</ref>. '''Ovotransferrin''' (OTF) is a glycosylated TF of egg white. For details see [[Molecular Playground/Transferrin]]. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | TF contains <scene name='48/480879/Cv/ | + | TF contains <scene name='48/480879/Cv/7'>two lobes</scene>: 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<ref>PMID:23256035</ref>. |
| - | *<scene name='48/480879/Cv/ | + | *<scene name='48/480879/Cv/8'>N-lobe Fe coordination site</scene>. |
| - | *<scene name='48/480879/Cv/ | + | *<scene name='48/480879/Cv/9'>C-lobe Fe coordination site</scene>. |
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== 3D Structures of Transferrin == | == 3D Structures of Transferrin == | ||
| + | [[Transferrin 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[1aov]] – dOTF<br /> | ||
| - | **[[1aiv]], [[1ryx]]– cOTF<br /> | ||
| - | **[[1tfa]] - cOTF N terminal<br /> | ||
| - | **[[1iq7]] - cOTF C terminal<br /> | ||
| - | **[[1lfc]] – OTF residues 17-41 – bovine - NMR | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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

