37VY
CTE Type I-like structure
Summary for 37VY
| Entry DOI | 10.2210/pdb37vy/pdb |
| EMDB information | 0527 78522 |
| Descriptor | Isoform Tau-F of Microtubule-associated protein tau (1 entity in total) |
| Functional Keywords | microtubule-associated protein, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 14 |
| Total formula weight | 642878.19 |
| Authors | |
| Primary citation | Watanabe, R.,Lee, E.B. Structural heterogeneity of CTE Type I tau filaments with an interface-shifted polymorph. Biochem.Biophys.Res.Commun., 838:154679-154679, 2026 Cited by PubMed Abstract: Tau filament types can differ in inter-protofilament packing while sharing the same protofilament fold. Motivated by our recent findings in vacuolar tauopathy, we analyzed cryo-electron microscopy (cryo-EM) data from brain-derived chronic traumatic encephalopathy (CTE) tau filaments deposited in EMPIAR-10313. We resolved the canonical CTE Type I structure and a previously unreported CTE Type I-like structure with a shifted protofilament interface at 2.78 and 2.96 Å, respectively. Mapping particle-state assignments back onto the original micrographs showed that the CTE Type I and CTE Type I-like packing states can occupy locally contiguous regions within the same fibrils. These findings identify an interface-shifted CTE Type I-like structure and support its local coexistence with CTE Type I within individual fibrils. PubMed: 42826653DOI: 10.1016/j.bbrc.2026.154679 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.96 Å) |
Structure validation
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