Journal article icon

Journal article

Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates

Abstract:

Peptide macrocycles are promising therapeutic molecules because they are protease resistant, structurally rigid, membrane permeable and capable of modulating protein-protein interactions. Here, we report the characterization of the dual function macrocyclase-peptidase enzyme involved in the biosynthesis of the highly toxic Amanitin toxin family of macrocycles. The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate. Conformational trapping of the 25 amino acid pepti...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

Actions


Access Document


Files:
Publisher copy:
10.1038/s41467-017-00862-4

Authors


More by this author
Department:
Oxford, MSD, NDM
Role:
Author
Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Communications Journal website
Volume:
8
Issue:
1045
Pages:
1-10
Publication date:
2017-10-19
Acceptance date:
2017-08-02
DOI:
ISSN:
2041-1723
Pubs id:
pubs:710162
URN:
uri:9319d7a6-06b5-48ca-94f6-9fe19bdc9295
UUID:
uuid:9319d7a6-06b5-48ca-94f6-9fe19bdc9295
Local pid:
pubs:710162

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP