28ms

X-ray structure of the adduct between human serum transferrin with Fe3+ bound at the C-lobe and dirhodium tetraacetate

spinqualitylabelsall models 28ms, resolution 2.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 28ms 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 2.37Å Ligands: ACT, FE, GOL, MLI, PEG 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 Ru and Rh binding sites in the structure of human serum transferrin with Fe(3+) bound at the C-lobe were identified by X-ray crystallography. Several His side chains and one Met are involved in the recognition of the metal ions by the protein. Ru and Rh binding sites in the structure of human serum transferrin with Fe(3+) bound at the C-lobe.,Banneville AS, Ferraro G, D'Elia R, Cornaciu-Hoffmann I, Pica A, Merlino A Dalton Trans. 2026 Mar 10;55(10):4051-4056. doi: 10.1039/d6dt00205f. PMID:41738634 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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