6KZU
Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled alpha-helical peptide modality
Summary for 6KZU
Entry DOI | 10.2210/pdb6kzu/pdb |
Descriptor | E3 ubiquitin-protein ligase Mdm2, 2JN-DAL-E03-DTY-2JN-DSG-TDF-DGL-MK8-DLE-DLE-2JN (3 entities in total) |
Functional Keywords | e3 ligase, ligase |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 15399.60 |
Authors | Jiang, S.,Brown, C.J. (deposition date: 2019-09-25, release date: 2019-10-16, Last modification date: 2023-11-22) |
Primary citation | 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. Macrocyclization of an all-d linear alpha-helical peptide imparts cellular permeability. Chem Sci, 11:5577-5591, 2020 Cited by PubMed: 32874502DOI: 10.1039/c9sc06383h PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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