Fig. 2: The Cryo-EM structure of the mC-hnRNPA2-LCD fibril core.
From: CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
a Domain structure of full-length hnRNPA2. The LCD (residues 181–341) is identified for structural determination. The gray bar shows the range of the ordered fibril core of the cryoEM structure. The red bar shows the core segment (crystal structure described below) containing the site of a disease-causing mutation. The magenta bar shows the nuclear localization signal, PY-NLS. The sequence of the ordered region is shown below with corresponding colors. b The mC-hnRNPA2-LCD fibril reconstruction, showing its left-handed twist and pitch. c Density and atomic model of one cross-sectional layer of the fibril. The box shows the aromatic triad. d Atomic model of one cross-sectional layer of the fibril. The predicted LARKS domain (contains 7 LARKS motifs) (above) and the shorter LARKS motif (below) are colored orange; the core segment is colored cyan, with its disease-causing mutation site colored red; the nuclear localization signal is colored magenta (lower left). β-sheet-forming residues are G274-N277, Y288-D290, P303-S306, S312-N314, indicated by arrows.
