We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Chemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27‐linked Ubiquitin Chains.
- Authors
Pan, Man; Zheng, Qingyun; Ding, Shan; Zhang, Lujia; Qu, Qian; Wang, Tian; Hong, Danning; Ren, Yujing; Liang, Lujun; Chen, Chunlai; Mei, Ziqing; Liu, Lei
- Abstract
New synthetic strategies that exploited the strengths of both chemoselective ligation and recombinant protein expression were developed to prepare K27 di‐ubiquitins (diUb), which enabled mechanistic studies on the molecular recognition of K27‐linked Ubs by single‐molecule Förster resonance energy transfer (smFRET) and X‐ray crystallography. The results revealed that free K27 diUb adopted a compact conformation, whereas upon binding to UCHL3, K27 diUb was remodeled to an open conformation. The K27 isopeptide bond remained rigidly buried inside the diUb moiety during binding, an interesting unique structural feature that may explain the distinctive biological function of K27 Ub chains.
- Subjects
CHEMOSELECTIVITY; RECOMBINANT proteins; PROTEIN expression; FLUORESCENCE resonance energy transfer; MOLECULAR recognition
- Publication
Angewandte Chemie, 2019, Vol 131, Issue 9, p2653
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201810814