8IB0
The amyloid structure of mouse RIPK1 RHIM-containing domain by solid-state NMR
Summary for 8IB0
| Entry DOI | 10.2210/pdb8ib0/pdb |
| Descriptor | Receptor-interacting serine/threonine-protein kinase 1 (1 entity in total) |
| Functional Keywords | necroptosis, ripk1, rhim, ssnmr, protein fibril |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 5 |
| Total formula weight | 13510.03 |
| Authors | Liu, J.,Xialian, W. (deposition date: 2023-02-09, release date: 2023-03-22, Last modification date: 2024-08-28) |
| Primary citation | Liu, J.,Wu, X.L.,Zhang, J.,Li, B.,Wang, H.Y.,Wang, J.,Lu, J.X. The structure of mouse RIPK1 RHIM-containing domain as a homo-amyloid and in RIPK1/RIPK3 complex. Nat Commun, 15:6975-6975, 2024 Cited by PubMed Abstract: Receptor-interacting protein kinase 1 (RIPK1) is a therapeutic target in treating neurodegenerative diseases and cancers. RIPK1 has three distinct functional domains, with the center domain containing a receptor-interacting protein homotypic interaction motif (RHIM), which mediates amyloid formation. The functional amyloid formed by RIPK1 and/or RIPK3 is a crucial intermediate in regulating cell necroptosis. In this study, the amyloid structure of mouse RIPK1, formed by an 82-residue sequence centered at RHIM, is presented. It reveals the "N"-shaped folding of the protein subunit in the fibril with four β-strands. The folding pattern is shared by several amyloid structures formed by proteins with RHIM, with the central β-strand formed by the most conserved tetrad sequence I/VQI/VG. However, the solid-state NMR results indicate a structural difference between mouse RIPK1 and mouse RIPK3. A change in the structural rigidity is also suggested by the observation of weakened signals for mouse RIPK3 upon mixing with RIPK1 to form the RIPK1/RIPK3 complex fibrils. Our results provide vital information to understand the interactions between different proteins with RHIM, which will help us further comprehend the regulation mechanism in cell necroptosis. PubMed: 39143113DOI: 10.1038/s41467-024-51303-y PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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