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pro vyhledávání: '"Melanie J. Adams"'
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The molecular mechanism of ubiquitin transfer from E1 to E2 enzymes is still unclear. By solving the crystal structure of a covalently trapped E1–E2–ubiquitin thioester mimetic, the authors identify two conformations of this complex which suggest
Externí odkaz:
https://doaj.org/article/e2f5ddd2897446a6b0118fb160ffec7e
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications
E1 enzymes function as gatekeepers of ubiquitin (Ub) signaling by catalyzing activation and transfer of Ub to tens of cognate E2 conjugating enzymes in a process called E1–E2 transthioesterification. The molecular mechanisms of transthioesterificat