The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers

Overview

Journal Acc Chem Res

Specialty Chemistry

Date 2006 Sep 20

PMID 16981672

Citations 55

Authors

David Eisenberg

Rebecca Nelson

Michael R Sawaya

Melinda Balbirnie

Shilpa Sambashivan

Magdalena I Ivanova

Anders O Madsen

Christian Riekel

Affiliations

Soon will be listed here.

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.

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