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Article

Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface.

The Journal of biological chemistry - 10 Aug 2012

DiCostanzo Ara Celi, Thompson James R, Peterson Francis C, Volkman Brian F, Ramirez-Alvarado Marina

Abstract excerpt

Light chain amyloidosis is an incurable protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amyloid fibrils, causing organ failure and death. Previously, we determined that amyloidogenic light chains AL-09 and AL-103 do not form fibrils at pH 10 (tyrosine pK(a)). There are three tyrosine residues (32, 91, and 96) clustered in the dimer interface, interacting differently...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22740699
DOI: 10.1074/jbc.M112.362921
PMCID: PMC3431636

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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