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Article

Structural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.

Biophysical journal - 21 Jul 2015

Zimmermann Michael T, Tischer Alexander, Whitten Steven T, Auton Matthew

Abstract excerpt

The von Willebrand factor (VWF) A1 and A3 domains are structurally isomorphic yet exhibit distinct mechanisms of unfolding. The A1 domain, responsible for platelet adhesion to VWF in hemostasis, unfolds through a molten globule intermediate in an apparent three-state mechanism, while A3 unfolds by a classical two-state mechanism. Inspection of the sequences or structures alone does not elucidate the source of...

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Identifiers

PMID: 26200876
DOI: 10.1016/j.bpj.2015.06.008
PMCID: PMC4621621

Genes

VWF

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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