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Atomic structures of corkscrew‐forming segments of SOD1 reveal varied oligomer conformations
Author(s) -
Sangwan Smriti,
Sawaya Michael R.,
Murray Kevin A.,
Hughes Michael P.,
Eisenberg David S.
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3391
Subject(s) - oligomer , chemistry , crystal structure , crystallography , protein structure , steric effects , amyloid fibril , fibril , biophysics , stereochemistry , biochemistry , biology , amyloid β , medicine , disease , organic chemistry , pathology
The aggregation cascade of disease‐related amyloidogenic proteins, terminating in insoluble amyloid fibrils, involves intermediate oligomeric states. The structural and biochemical details of these oligomers have been largely unknown. Here we report crystal structures of variants of the cytotoxic oligomer‐forming segment residues 28–38 of the ALS‐linked protein, SOD1. The crystal structures reveal three different architectures: corkscrew oligomeric structure, nontwisting curved sheet structure and a steric zipper proto‐filament structure. Our work highlights the polymorphism of the segment 28–38 of SOD1 and identifies the molecular features of amyloidogenic entities.