A new crystal form of Lys48-linked diubiquitin

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A new crystal form of Lys48-linked diubiquitin

Lys48-linked polyubiquitin chains are recognized by the proteasome as a tag for the degradation of the attached substrates. Here, a new crystal form of Lys48-linked diubiquitin (Ub2) was obtained and the crystal structure was refined to 1.6 A resolution. The structure reveals an ordered isopeptide bond in a trans configuration. All three molecules in the asymmetric unit were in the same closed ...

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An E2 dimer simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains

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Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain.

Although functional diversity in polyubiquitin chain signaling has been ascribed to the ability of differently linked chains to bind in a distinctive manner to effector proteins, structural models of such interactions have been lacking. Here, we use NMR to unveil the structural basis of selective recognition of Lys48-linked di- and tetraubiquitin chains by the UBA2 domain of hHR23A. Although th...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications

سال: 2010

ISSN: 1744-3091

DOI: 10.1107/s1744309110027600