Supplementary Figure 9: RACs in the structure of the FUS LC fibril core.
From: Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation
(a) Superposition of the 20 low-energy solid state NMR structural models of one FUS (37–97) molecule (PDB ID:5W3N). The fibril axis was indicated. The main chain conformation of FUS (37–97) is shown. RAC1 and RAC2 are highlighted in red. RAC1 and RAC2 are the most flexible regions in the structure. Segments 84SQSSQS89 and 90SYGQQS95 that are involved in the stable core of FUS (37–97) are highlighted in blue and cyan, respectively. (b) Segments 84SQSSQS89 and 90SYGQQS95 form thermostable crystal-like fibril bundles imaged by TEM. (c) Clouding points of LC variants (deletions of 84SQSSQS89 and 90SYGQQS95, respectively) from phase separation diagrams measured at the protein concentration of 150 μM. Data shown are means and s.d. of n = 3 biologically independent samples. Values were compared using Student’s t-test. “NS” represents “non-significant”.
