Fig. 6 | Nature Communications

Fig. 6

From: Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

Fig. 6

Point mutations and their effect on fibril elongation rates. a Top view of a PI3K-SH3 monomer derived from DF fibrils. Highlighted residues: Isoleucine residues mutated to alanine (I22A, I29A, I53A, I77A, I82A), from this work (red) and charged residues mutated by Buell et al.47 (K16Q, E52K, E61K, pink). Mutation I82A is missing in the model due to the flexible C-terminus. b Elongation rate of Ile-to-Ala mutants. The elongation rates are normalised to a WT rate of one. Source data are provided as a Source Data file

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