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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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Autori principali: Berndsen, Christopher E., Wiener, Reuven, Yu, Ian W., Ringel, Alison E., Wolberger, Cynthia
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2013
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Accesso online: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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