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FEBS Lett. 2009 Aug 20;583(16):2623-9. doi: 10.1016/j.febslet.2009.05.005. Epub 2009 May 9.

Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape.

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1
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.

Abstract

Beta(2)-microglobulin (beta(2)m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled from beta(2)m under both low pH conditions, where the precursor is disordered, and at neutral pH where the protein is initially natively folded. Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of beta(2)m at both low and neutral pH, and the common and distinct features of these assembly pathways.

PMID:
19433089
PMCID:
PMC2734061
DOI:
10.1016/j.febslet.2009.05.005
[Indexed for MEDLINE]
Free PMC Article
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