Crystal structure of the Ube2K/E2-25K and K48-linked di-ubiquitin complex provides structural insight into the mechanism of K48-specific ubiquitin chain synthesis.
Sign Up to like & getrecommendations! Published in 2018 at "Biochemical and biophysical research communications"
DOI: 10.1016/j.bbrc.2018.10.067
Abstract: Ubiquitin-conjugating enzymes (E2) form thioester bonds with ubiquitin (Ub), which are subsequently transferred to target proteins for cellular progress. Ube2K/E2-25K (a class II E2 enzyme) contains a C-terminal ubiquitin-associated (UBA) domain that has been suggested… read more here.
Keywords: crystal structure; k48; ube2k 25k; k48 linked ... See more keywords
An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure.
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DOI: 10.1016/j.str.2020.02.007
Abstract: Rpn13/Adrm1 is recruited to the proteasome by PSMD1/Rpn2, where it serves as a substrate receptor that binds preferentially to K48-linked ubiquitin chains, an established signal for protein proteolysis. Here, we use NMR to solve the… read more here.
Keywords: k48; conformation; structure; k48 diubiquitin ... See more keywords
Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination
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DOI: 10.1038/s41467-025-59569-6
Abstract: The K29/K48-linked ubiquitination generated by the cooperative catalysis of E3 ligase Ufd4 and Ubr1 is an enhanced protein degradation signal, in which Ufd4 is responsible for introducing K29-linked ubiquitination to K48-linked ubiquitin chains to augment… read more here.
Keywords: hect; ligase ufd4; k48; k29 k48 ... See more keywords