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Acc Chem Res. 2006 Sep;39(9):568-75.

The structural biology of protein aggregation diseases: Fundamental questions and some answers.

Author information

1
Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA. david@mbi.ucla.edu

Abstract

Amyloid fibrils are found in association with at least two dozen fatal diseases. The tendency of numerous proteins to convert into amyloid-like fibrils poses fundamental questions for structural biology and for protein science in general. Among these are the following: What is the structure of the cross-beta spine, common to amyloid-like fibrils? Is there a sequence signature for proteins that form amyloid-like fibrils? What is the nature of the structural conversion from native to amyloid states, and do fibril-forming proteins have two distinct stable states, the native state and the amyloid state? What is the basis of protein complementarity, in which a protein chain can bind to itself? We offer tentative answers here, based on our own recent structural studies.

PMID:
16981672
PMCID:
PMC3017558
DOI:
10.1021/ar0500618
[Indexed for MEDLINE]
Free PMC Article
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