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Nat Methods. 2016 Nov;13(11):925-927. doi: 10.1038/nmeth.4004. Epub 2016 Sep 26.

Enzyme-catalyzed expressed protein ligation.

Author information

  • 1Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, Maryland, USA.
  • 2Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
  • 3Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, California, USA.

Abstract

Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-terminal cysteine (N-Cys)-containing peptides, but the requirement of a Cys residue at the ligation junction can limit the utility of this method. Here we employ subtiligase variants to efficiently ligate Cys-free peptides to protein thioesters. Using this method, we have more accurately determined the effect of C-terminal phosphorylation on the tumor suppressor protein PTEN.

PMID:
27669326
PMCID:
PMC5088058
[Available on 2017-03-26]
DOI:
10.1038/nmeth.4004
[PubMed - in process]
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