Ontology highlight
ABSTRACT:
SUBMITTER: Sangwan S
PROVIDER: S-EPMC6032342 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
Sangwan Smriti S Sawaya Michael R MR Murray Kevin A KA Hughes Michael P MP Eisenberg David S DS
Protein science : a publication of the Protein Society 20180310 7
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 a ...[more]