1.
Exp Hematol
; 42(1): 11-3, 2014 Jan.
Artigo
em Inglês
| MEDLINE
| ID: mdl-24096121
2.
Nat Chem Biol
; 9(3): 154-6, 2013 Mar.
Artigo
em Inglês
| MEDLINE
| ID: mdl-23292652
RESUMO
It is widely accepted that ubiquitin-conjugating enzymes 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 the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop.