New insights into ubiquitin E3 ligase mechanism

Christopher E. Berndsen, Cynthia Wolberger

Research output: Contribution to journalArticle

Abstract

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.

Original languageEnglish (US)
Pages (from-to)301-307
Number of pages7
JournalNature structural & molecular biology
Volume21
Issue number4
DOIs
StatePublished - 2014

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Ubiquitin-Protein Ligases
Ubiquitin
Ubiquitins
Ubiquitination
Lysine
Enzymes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

New insights into ubiquitin E3 ligase mechanism. / Berndsen, Christopher E.; Wolberger, Cynthia.

In: Nature structural & molecular biology, Vol. 21, No. 4, 2014, p. 301-307.

Research output: Contribution to journalArticle

Berndsen, Christopher E. ; Wolberger, Cynthia. / New insights into ubiquitin E3 ligase mechanism. In: Nature structural & molecular biology. 2014 ; Vol. 21, No. 4. pp. 301-307.
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