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A conserved asparagine plays a structural role in ubiquitin-conjugating enzymes
It is widely accepted that ubiquitin conjugating enzymes (E2) contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of t...
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| Glavni autori: | , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
2013
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| Teme: | |
| Online pristup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3578109/ https://ncbi.nlm.nih.gov/pubmed/23292652 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nchembio.1159 |
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