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Article

The beta-strand D of transthyretin trapped in two discrete conformations.

Biochimica et biophysica acta - 1 Jul 2004

Hörnberg Andreas, Olofsson Anders, Eneqvist Therese, Lundgren Erik, Sauer-Eriksson A Elisabeth

Abstract excerpt

Conformational changes in native and variant forms of the human plasma protein transthyretin (TTR) induce several types of amyloid diseases. Biochemical and structural studies have mapped the initiation site of amyloid formation onto residues at the outer C and D beta-strands and their connecting loop. In this study, we characterise an engineered variant of transthyretin, Ala108Tyr/Leu110Glu, which is kinetically...

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Source

Identifiers

PMID: 15210129
DOI: 10.1016/j.bbapap.2004.04.004

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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