fig1

Newly identified transmembrane protein 106B amyloid fibrils in the human brain: pathogens or by-products?

Figure 1. Polymorphs of ex vivo TMEM106B fibrils. A: Singlet of ex vivo TMEM106B polymorphs. The residues with glycosylation, N145, N151, N164, and N183, are highlighted in cyan. The dashed oval indicates the disulfide bond between C214 and C253; B: Doublet of ex vivo TMEM106B polymorphs. The residues comprising the interface of D-Ia and D-Ib are highlighted in yellow and orange, respectively. The blue oral indicates the unknown density comprising the D-Ia interface; C: Overlay of Folds I, IIa, IIb, and III. The N-terminal region (S120-T166), the middle region (A167-M210), and the C-terminal region (Y211-G254) of the three folds are indicated by different transparency. Side chains in (A) and (B) are shown as sticks.

Ageing and Neurodegenerative Diseases
ISSN 2769-5301 (Online)

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