7DAC
Human RIPK3 amyloid fibril revealed by solid-state NMR
Summary for 7DAC
| Entry DOI | 10.2210/pdb7dac/pdb |
| Descriptor | Receptor-interacting serine/threonine-protein kinase 3 (1 entity in total) |
| Functional Keywords | programmed necrosis, amyloid, protein fibril |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 5 |
| Total formula weight | 59315.36 |
| Authors | Wu, X.L.,Zhang, J.,Dong, X.Q.,Liu, J.,Li, B.,Hu, H.,Wang, J.,Wang, H.Y.,Lu, J.X. (deposition date: 2020-10-16, release date: 2021-04-28, Last modification date: 2024-05-01) |
| Primary citation | Wu, X.,Ma, Y.,Zhao, K.,Zhang, J.,Sun, Y.,Li, Y.,Dong, X.,Hu, H.,Liu, J.,Wang, J.,Zhang, X.,Li, B.,Wang, H.,Li, D.,Sun, B.,Lu, J.,Liu, C. The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: Receptor-interacting protein kinases 3 (RIPK3), a central node in necroptosis, polymerizes in response to the upstream signals and then activates its downstream mediator to induce cell death. The active polymeric form of RIPK3 has been indicated as the form of amyloid fibrils assembled via its RIP homotypic interaction motif (RHIM). In this study, we combine cryogenic electron microscopy and solid-state NMR to determine the amyloid fibril structure of RIPK3 RHIM-containing C-terminal domain (CTD). The structure reveals a single protofilament composed of the RHIM domain. RHIM forms three β-strands (referred to as strands 1 through 3) folding into an S shape, a distinct fold from that in complex with RIPK1. The consensus tetrapeptide VQVG of RHIM forms strand 2, which zips up strands 1 and 3 via heterozipper-like interfaces. Notably, the RIPK3-CTD fibril, as a physiological fibril, exhibits distinctive assembly compared with pathological fibrils. It has an exceptionally small fibril core and twists in both handedness with the smallest pitch known so far. These traits may contribute to a favorable spatial arrangement of RIPK3 kinase domain for efficient phosphorylation. PubMed: 33790016DOI: 10.1073/pnas.2022933118 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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