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- W2094399210 abstract "Molecular modelling techniques have been used to calculate thestructure for the primary, mammalian copper-containing protein,metallothionein Cu 12-MT. Structural information obtained fromexisting spectroscopic data and comparison with inorganiccopper(I)–thiolate model compounds were employed. Atwo-domain structure, with stoichiometries of Cu 6S 9 and Cu 6S 11, was constructed in which thecopper(I)–cysteine connections were based on thearrangement of the cysteines in the Zn 7-MT precursor asdetermined by previous 1H NMR studies. In the minimizedstructure, in which metal–thiolate bond lengths and angles wereallowed to vary, each copper(I) was trigonally co-ordinatedby cysteine thiolates; the average bond length was calculated to beclose to 224 pm. In the α domain of the protein both bridging (7S)and terminal (4S) thiolate ligation take part in theCu 6S 11 cluster structure, in the β domain allnine thiolates bridge pairs of Cu I atoms to form theCu 6S 9 cluster structure. Significantly, theenergy-minimized structure exhibits two main crevices that are similarto those reported for the structure of Cd 5Zn 2-MT 1obtained by analysis of X-ray diffraction data. These crevices couldallow access to the otherwise embedded copper–thiolateclusters." @default.
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- W2094399210 date "1997-01-01" @default.
- W2094399210 modified "2023-09-26" @default.
- W2094399210 title "Structural model of rabbit liver copper metallothionein" @default.
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- W2094399210 doi "https://doi.org/10.1039/a605462e" @default.
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