9HR9
SSNMR structure of amyloid fibrils formed by human RIPK1
Summary for 9HR9
| Entry DOI | 10.2210/pdb9hr9/pdb |
| Related | 9HR6 |
| NMR Information | BMRB: 34971 |
| Descriptor | Receptor-interacting serine/threonine-protein kinase 1 (1 entity in total) |
| Functional Keywords | amyloid, kinase, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 2513.84 |
| Authors | Polonio, P.,Escobedo-Gonzales, F.C.,Titaux-Delgado, G.A.,Mompean, M. (deposition date: 2024-12-17, release date: 2025-09-17, Last modification date: 2025-10-22) |
| Primary citation | Polonio, P.,Mompean, M. Resonance assignments of the human receptor interacting protein kinase 1 (RIPK1) in its fibrillar conformation. Biomol.Nmr Assign., 19:299-304, 2025 Cited by PubMed Abstract: Receptor-interacting protein kinase 1 (RIPK1) is a key regulator of necroptotic signalling that forms functional amyloid fibrils through its RIP Homotypic Interaction Motif (RHIM). Here, we report the solid-state NMR chemical shift assignments for the rigid amyloid core of human RIPK1 fibrils, encompassing residues 529-552 within the RHIM. Assignments were obtained from uniformly C,N-labeled protein diluted with unlabeled protein and measured using cross-polarization magic angle spinning (CPMAS) experiments on a cryogenic probe. The dataset includes backbone and side-chain resonances for the ordered region and provides a basis for high-resolution structural and dynamics studies of RIPK1 and related RHIM-containing assemblies. PubMed: 40952585DOI: 10.1007/s12104-025-10249-y PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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