Transferrin

(Difference between revisions)

Revision as of 12:40, 25 September 2019

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

Drag the structure with the mouse to rotate

Updated on 25-September-2019

↑ 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

@@ Line 8: / Line 8: @@
 == Structural highlights ==
-TF contains <scene name='48/480879/Cv/2'>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>.
+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/5'>N-lobe Fe coordination</scene>.
+*<scene name='48/480879/Cv/8'>N-lobe Fe coordination site</scene>.
-*<scene name='48/480879/Cv/6'>C-lobe Fe coordination</scene>.
+*<scene name='48/480879/Cv/9'>C-lobe Fe coordination site</scene>.
 </StructureSection>
 == 3D Structures of Transferrin ==