The interaction of sodium aurothiomalate with the apo form of human serum transferrin(hTF)was studied by X-ray crystallography.The protein binds gold ions close to the side chains of His25,Asp63 and His249,His207 and ...The interaction of sodium aurothiomalate with the apo form of human serum transferrin(hTF)was studied by X-ray crystallography.The protein binds gold ions close to the side chains of His25,Asp63 and His249,His207 and Tyr238,and His273,His289,His300,His473,His585,His598,His606,and His642;the thiomalate ligand is released.Notably,the N-and C-lobes of one of the two hTF molecules in the asymmetric unit of the Au-hTF adduct crystals exhibit conformations that are slightly different from those observed in the“fully opened”apo-hTF,with the N-lobe that is intermediate between the“partially opened”form observed in the structure of hTF with Bi^(3+) and the“fully opened”form of apo-hTF.Thus,our data provide relevant information about the binding of gold centers to hTF and on a unique hTF structure along the apo-hTF/holo-hTF transition pathway.展开更多
基金supported with a research fellowship by#NEXTGENERATIONEU(NGEU)the Ministry of University and Research(MUR),the National Recovery and Resilience Plan(NRRP),project MNESYS(PE0000006)-A Multiscale integrated approach to the study of the nervous system in health and disease(DN.155311.10.2022)MIUR PRIN 2022-Cod.2022JMFC3X,“Protein Metalation by Anticancer Metal-based Drugs”for financial support.
文摘The interaction of sodium aurothiomalate with the apo form of human serum transferrin(hTF)was studied by X-ray crystallography.The protein binds gold ions close to the side chains of His25,Asp63 and His249,His207 and Tyr238,and His273,His289,His300,His473,His585,His598,His606,and His642;the thiomalate ligand is released.Notably,the N-and C-lobes of one of the two hTF molecules in the asymmetric unit of the Au-hTF adduct crystals exhibit conformations that are slightly different from those observed in the“fully opened”apo-hTF,with the N-lobe that is intermediate between the“partially opened”form observed in the structure of hTF with Bi^(3+) and the“fully opened”form of apo-hTF.Thus,our data provide relevant information about the binding of gold centers to hTF and on a unique hTF structure along the apo-hTF/holo-hTF transition pathway.
