The Structural Mechanism for IronUptake JSBA and Release by Transferrins Masaaki HiRosE
نویسنده
چکیده
tebrates by their abi}ity to bind tvvo Fe3' and two CO;-. The transfenin molecule, with a mo]ecu)ar mass of about 80 kDa, is folded into two similarly sized homologous Nand C-lobes that are stabilized by many intrachain disulfides. As observed by X-ray crystallography, each lobe is further diyided into two similarly sized domains, domain 1 and domain 2, and an Fe3+binding site is within the interdomain cleft. Four of the six Fe3+ coordination sites are occupied by protein ligands (2 Tyr residues, 1 Asp, and 1 His) and the other two by a bidentate COI-. Upon uptake and release of Fe3+ , transferrins undergo a large-scale conformational
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