8brc
From Proteopedia
Crystal structure of the adduct between human serum transferrin and cisplatin
Structural highlights
DiseaseTRFE_HUMAN Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.[1] [2] FunctionTRFE_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. Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Ferraro G | Galardo F | Merlino A | Sica F | Troisi R
