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Article

D-strand perturbation and amyloid propensity in beta-2 microglobulin.

The FEBS journal - 1 Jul 2011

Azinas Stavros, Colombo Matteo, Barbiroli Alberto, Santambrogio Carlo, Giorgetti Sofia, Raimondi Sara, Bonomi Francesco, Grandori Rita, Bellotti Vittorio, Ricagno Stefano, Bolognesi Martino

Abstract excerpt

Proteins hosting main β-sheets adopt specific strategies to avoid intermolecular interactions leading to aggregation and amyloid deposition. Human beta-2 microglobulin (β2m) displays a typical immunoglobulin fold and is known to be amyloidogenic in vivo. Upon severe kidney deficiency, β2m accumulates in the bloodstream, triggering, over the years, pathological deposition of large amyloid aggregates in joints and...

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Share to Amyloid
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Crystallography, X-Ray

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Share to Protein Folding

Share to Protein Structure, Secondary

Share to Spectrometry, Mass, Electrospray Ionization

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Identifiers

PMID: 21569201
DOI: 10.1111/j.1742-4658.2011.08157.x

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