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TitleScreening macrocyclic peptide libraries by yeast display allows control of selection process and affinity ranking.
Journal, issue, pagesNat Commun, Vol. 16, Page 5367-5367, Year 2025
Publish dateMay 1, 2024 (structure data deposition date)
AuthorsLinciano, S. / Mazzocato, Y. / Romanyuk, Z. / Vascon, F. / Farrera-Soler, L. / Will, E. / Xing, Y. / Chen, S. / Kumada, Y. / Simeoni, M. ...Linciano, S. / Mazzocato, Y. / Romanyuk, Z. / Vascon, F. / Farrera-Soler, L. / Will, E. / Xing, Y. / Chen, S. / Kumada, Y. / Simeoni, M. / Scarso, A. / Cendron, L. / Heinis, C. / Angelini, A.
External linksNat Commun / PubMed:40562762
MethodsX-ray diffraction
Resolution2.42 Å
Structure data

PDB-9f6h:
Crystal structure of bovine alpha-chymotrypsin in complex with the bicyclic peptide inhibitor MP5.4.3
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bos taurus (domestic cattle)
  • synthetic construct (others)
KeywordsHYDROLASE / Serine protease; Bicyclic peptide

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