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Article

DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.

Protein science : a publication of the Protein Society - 1 Jul 2010

Santambrogio Carlo, Ricagno Stefano, Colombo Matteo, Barbiroli Alberto, Bonomi Francesco, Bellotti Vittorio, Bolognesi Martino, Grandori Rita

Abstract excerpt

Beta2 microglobulin (beta2m) is the light chain of class-I major histocompatibility complex (MHC-I). Its accumulation in the blood of patients affected by kidney failure leads to amyloid deposition around skeletal joints and bones, a severe condition known as Dialysis Related Amyloidosis (DRA). In an effort to dissect the structural determinants of beta2m aggregation, several beta2m mutants have been previously...

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Identifiers

PMID: 20506535
DOI: 10.1002/pro.419
PMCID: PMC2974830

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Source receipt: pubmed, retrieved 7 Sept 2026.

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DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.PMID 20506535Read ↗

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Role of conformational change in the C-terminus of beta2-microglobulin in dialysis-related amyloidosis.Semantic proximity Read ↗

Structure, stability, and aggregation of β-2 microglobulin mutants: insights from a Fourier transform infrared study in solution and in the crystalline state.Semantic proximity Read ↗

A Self-Consistent Molecular Mechanism of β2-Microglobulin Aggregation.Semantic proximity Read ↗

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Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architecture.Semantic proximity Read ↗

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