UFC1 reveals the multifactorial and plastic nature of oxyanion holes in E2 conjugating enzymes
UFC1 reveals the multifactorial and plastic nature of oxyanion holes in E2 conjugating enzymes
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
The conjugation of ubiquitin (Ub) or ubiquitin-like proteins (UBL) to target proteins is a crucial post-translational modification that typically involves nucleophilic attack by a lysine on a charged E2 enzyme (E2~Ub/UBL), forming an oxyanion intermediate. Stabilizing this intermediate through an oxyanion hole is vital for progression of the reacti...
Alternative Titles
Full title
UFC1 reveals the multifactorial and plastic nature of oxyanion holes in E2 conjugating enzymes
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_8ce92024ecbb4b999ab96bf0543e5960
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8ce92024ecbb4b999ab96bf0543e5960
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-025-58826-y
