8brc
From Proteopedia
(Difference between revisions)
| Line 12: | Line 12: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. | [https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The molecular mechanism of how human serum transferrin (hTF) recognizes cisplatin at the atomic level is still unclear. Here, we report the molecular structure of the adduct formed upon the reaction of hTF with cisplatin. Pt binds the side chain of Met256 (at the N-lobe), without altering the protein overall conformation. | ||
| + | |||
| + | Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study.,Troisi R, Galardo F, Ferraro G, Sica F, Merlino A Inorg Chem. 2023 Jan 16;62(2):675-678. doi: 10.1021/acs.inorgchem.2c04206. Epub , 2023 Jan 5. PMID:36602395<ref>PMID:36602395</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8brc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal structure of the adduct between human serum transferrin and cisplatin
| |||||||||||
Categories: Homo sapiens | Large Structures | Ferraro G | Galardo F | Merlino A | Sica F | Troisi R
