8brc

Crystal structure of the adduct between human serum transferrin and cisplatin

spinqualitylabelsall models 8brc, resolution 3.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8brc is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.17Å Ligands: FE, MLI, NAG, NH3, PT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease TRFE_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. Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin 3D structures

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