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Article

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.

Science (New York, N.Y.) - 16 Aug 2002

Huizinga Eric G, Tsuji Shizuko, Romijn Roland A P, Schiphorst Marion E, de Groot Philip G, Sixma Jan J, Gros Piet

Abstract excerpt

Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites of vascular damage and play a role in haemostasis and thrombosis. Here we present structures of the GpIbalpha amino-terminal domain and its complex with the VWF domain A1. In the complex, GpIbalpha wraps around one side of A1, providing two contact areas...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 12183630
DOI: 10.1126/science.107355

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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Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.PMID 12183630Read ↗

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A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.Semantic proximity Read ↗

Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stress.Semantic proximity Read ↗

Structural basis of regulation of von Willebrand factor binding to glycoprotein Ib.Semantic proximity Read ↗

Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib.Semantic proximity Read ↗

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