Fig. 4: Structural comparison of ATTRv-I84S fibril models.
From: Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy
a Pairwise r.m.s.d. comparison (Cα) between the different folds from ATTRv-I84S patients, showing major structural deviations in the gate region and more subtle changes across the protein. The missing region in all fibrils are marked with a dashed rectangle. The residues that contribute to the gate are highlighted in sea green. The top panel depicts the linear secondary structure of the tetrameric transthyretin in its native and functional form. Letters represent distinct β strands. b, c Location of the missing region and the gate region in the native transthyretin tetramer (b) and monomer (c) structure. PDB, 4TLT. Residues Gly 1 to Lys 9 are missing in the structures of both tetrameric and amyloid transthyretin.
