IndraLab

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BAP1 binds TG2-179-1. 3 / 3
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"We therefore propose that the covalent interaction between BAP1 and TG2-179-1 is reversible."
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"These data clearly demonstrated that TG2-179-1 inhibits the DUB activity of BAP1.Analysis of the structural model of the BAP1–TG2-179-1 complex using the CavityPlus server showed that Cys91 was predicted to form a covalent bond with an electron-deficient atom in TG2-179-1 ."
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"Our in silico docking model predicted that TG2-179-1 binds to BAP1 with its fluorobenzene and thiolane rings deeply embedded into the active site pocket, which sterically allows TG2-179-1 to interact covalently with Cys91 in the active site via its electrophilic nitrile carbon atom."
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