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- W2110119945 abstract "Most blood plasma zinc is bound to albumin, but the structure of the binding site has not been determined. Zn K-edge extended x-ray absorption fine structure spectroscopy and modeling studies show that the major Zn(2+) site on albumin is a 5-coordinate site with average Zn-O/N distances of 1.98 A and a weak sixth O/N bond of 2.48 A, consistent with coordination to His(67) and Asn(99) from domain I, His(247) and Asp(249) from domain II (residues conserved in all sequenced mammalian albumins), plus a water ligand. The dynamics of the domain I/II interface, thought to be important to biological function, are affected by Zn(2+) binding, which induces cooperative allosteric effects related to those of the pH-dependent neutral-to-base transition. N99D and N99H mutations enhance Zn(2+) binding but alter protein stability, whereas mutation of His(67) to alanine removes an interdomain H-bond and weakens Zn(2+) binding. Both wild-type and mutant albumins promote the safe management of high micromolar zinc concentrations for cells in cultures." @default.
- W2110119945 created "2016-06-24" @default.
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- W2110119945 date "2009-08-01" @default.
- W2110119945 modified "2023-10-18" @default.
- W2110119945 title "Structure, Properties, and Engineering of the Major Zinc Binding Site on Human Albumin" @default.
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- W2110119945 doi "https://doi.org/10.1074/jbc.m109.003459" @default.
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- W2110119945 hasPublicationYear "2009" @default.
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