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Article

Structural insight into pH-induced conformational changes within the native human transthyretin tetramer.

Journal of molecular biology - 24 Oct 2008

Palaninathan Satheesh K, Mohamedmohaideen Nilofar N, Snee William C, Kelly Jeffery W, Sacchettini James C

Abstract excerpt

Acidification of the transthyretin (TTR) tetramer facilitates dissociation and conformational changes in the protein, allowing alternatively folded monomers to self-assemble into insoluble amyloid fibers by a downhill polymerization mechanism in vitro. To investigate the influence of acidification on the quaternary and tertiary structures of TTR, crystal structures of wild-type human TTR at pH 4.0 and pH 3.5 have...

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

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Share to Protein Structure, Quaternary

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Source

Identifiers

PMID: 18662699
DOI: 10.1016/j.jmb.2008.07.029

Genes

TTR

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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