Amyloid Structure: Conformational Diversity and Consequences
- 7 July 2011
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biochemistry
- Vol. 80 (1), 557-585
- https://doi.org/10.1146/annurev-biochem-090908-120656
Abstract
Many, perhaps most, proteins, are capable of forming self-propagating, β-sheet (amyloid) aggregates. Amyloid-like aggregates are found in a wide range of diseases and underlie prion-based inheritance. Despite intense interest in amyloids, structural details have only recently begun to be revealed as advances in biophysical approaches, such as hydrogen-deuterium exchange, X-ray crystallography, solid-state nuclear magnetic resonance (SSNMR), and cryoelectron microscopy (cryoEM), have enabled high-resolution insights into their molecular organization. Initial studies found that despite the highly divergent primary structure of different amyloid-forming proteins, amyloids from different sources share many structural similarities. With higher-resolution information, however, it has become clear that, on the molecular level, amyloids comprise a wide diversity of structures. Particularly surprising has been the finding that identical polypeptides can fold into multiple, distinct amyloid conformations and that this structural diversity can lead to distinct heritable prion states or strains.Keywords
This publication has 136 references indexed in Scilit:
- Differences in prion strain conformations result from non-native interactions in a nucleusNature Chemical Biology, 2010
- Molecular mechanisms for protein-encoded inheritanceNature Structural & Molecular Biology, 2009
- Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid FibrilsBiochemistry, 2009
- Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMRBiochemistry, 2007
- Prions of fungi: inherited structures and biological rolesNature Reviews Microbiology, 2007
- Atomic structures of amyloid cross-β spines reveal varied steric zippersNature, 2007
- The physical basis of how prion conformations determine strain phenotypesNature, 2006
- Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid FibrilsBiochemistry, 2005
- Correlation of structural elements and infectivity of the HET-s prionNature, 2005
- Structure of the cross-β spine of amyloid-like fibrilsNature, 2005