Fig. 4: Additional hydrogen bond in G175S alters packing. | Nature Communications

Fig. 4: Additional hydrogen bond in G175S alters packing.

From: Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome

Fig. 4

a Packing schemes of one cross-sectional layer of the fibrils, illustrating the structural arrangement of residues in wild-type and G175S mutant fibrils. Asterisks (*) indicate the inner cavities present in Polymorph 2 and G175S. Blue and red circles and arrowheads highlight the positions of Tyr159 and Gly/Ser175, respectively. Numbers of key residues are labeled. Residues are color-coded by chemical properties: hydrophobic (white), polar (green), basic (blue), glycine (magenta), and proline (purple). b Close-up views of the G175S fibril highlighting the additional hydrogen bond formed between Tyr159 and Ser175. Insets show the cross-sectional orientation of the fibril and the corresponding regions displayed in the top view (top) and side view (bottom).

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