7W36
Crystal structure of human Atg5 complexed with a stapled peptide
Summary for 7W36
| Entry DOI | 10.2210/pdb7w36/pdb |
| Descriptor | Autophagy protein 5, Stapled ATG16L1-derived peptide (2 entities in total) |
| Functional Keywords | autophagy, inhibitor, complex, stapled peptide, ligase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 35314.48 |
| Authors | Kurata, I.,Matoba, K.,Noda, N.N. (deposition date: 2021-11-25, release date: 2022-09-21, Last modification date: 2024-10-16) |
| Primary citation | Cui, J.,Ogasawara, Y.,Kurata, I.,Matoba, K.,Fujioka, Y.,Noda, N.N.,Shibasaki, M.,Watanabe, T. Targeting the ATG5-ATG16L1 Protein-Protein Interaction with a Hydrocarbon-Stapled Peptide Derived from ATG16L1 for Autophagy Inhibition. J.Am.Chem.Soc., 144:17671-17679, 2022 Cited by PubMed Abstract: Selective modulation of autophagy is a promising therapeutic strategy, especially for cancer treatment. However, the lack of specific autophagy inhibitors limits this strategy. The formation of the ATG12-ATG5-ATG16L1 complex is essential for targeting the ATG12-ATG5 conjugate to proper membranes and to generate LC3-II for the progression of autophagy. Thus, targeting ATG5-ATG16L1 protein-protein interactions (PPIs) might inhibit early stage autophagy with high specificity. In this paper, we report that a stapled peptide derived from ATG16L1 exhibits potent binding affinity to ATG5, striking resistance to proteolysis, and significant autophagy inhibition activities in cells. PubMed: 36107218DOI: 10.1021/jacs.2c07648 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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