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Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780.

New insights into ubiquitin E3 ligase mechanism.

Author information

1
Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, USA.
2
1] Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. [2] Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.

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.

PMID:
24699078
DOI:
10.1038/nsmb.2780
[Indexed for MEDLINE]

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