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TitleMacrocyclization of an all-d linear alpha-helical peptide imparts cellular permeability.
Journal, issue, pagesChem Sci, Vol. 11, Page 5577-5591, Year 2020
Publish dateSep 25, 2019 (structure data deposition date)
AuthorsKannan, S. / Aronica, P.G.A. / Ng, S. / Gek Lian, D.T. / Frosi, Y. / Chee, S. / Shimin, J. / Yuen, T.Y. / Sadruddin, A. / Kaan, H.Y.K. ...Kannan, S. / Aronica, P.G.A. / Ng, S. / Gek Lian, D.T. / Frosi, Y. / Chee, S. / Shimin, J. / Yuen, T.Y. / Sadruddin, A. / Kaan, H.Y.K. / Chandramohan, A. / Wong, J.H. / Tan, Y.S. / Chang, Z.W. / Ferrer-Gago, F.J. / Arumugam, P. / Han, Y. / Chen, S. / Renia, L. / Brown, C.J. / Johannes, C.W. / Henry, B. / Lane, D.P. / Sawyer, T.K. / Verma, C.S. / Partridge, A.W.
External linksChem Sci / PubMed:32874502
MethodsX-ray diffraction
Resolution1.79 Å
Structure data

PDB-6kzu:
Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled alpha-helical peptide modality
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • phage 13 (virus)
KeywordsLIGASE / E3 ligase

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