4.4 Article

Structure of a compact conformation of linear diubiquitin

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WILEY-BLACKWELL
DOI: 10.1107/S0907444911051195

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linear ubiquitin chain; diubiquitin; ubiquitin-binding domains; NF-?B essential modulator

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  1. MEXT

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Post-translational modifications involving ubiquitin regulate a wide range of biological processes including protein degradation, responses to DNA damage and immune signalling. Ubiquitin polymerizes into chains which may contain eight different linkage types; the ubiquitin C-terminal glycine can link to one of the seven lysine residues or the N-terminal amino group of methionine in the distal ubiquitin molecule. The latter head-to-tail linkage type, referred to as a linear ubiquitin chain, is involved in NF-B activation through specific interactions with NF-?B essential modulator (NEMO). Here, a crystal structure of linear diubiquitin at a resolution of 2.2 angstrom is reported. Although the two ubiquitin moieties do not interact with each other directly, the overall structure adopts a compact but not completely closed conformation with a few intermoiety contacts. This structure differs from the previously reported extended conformation, which resembles Lys63-linked diubiquitin, suggesting that the linear polyubiquitin chain is intrinsically flexible and can adopt multiple conformations.

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