Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 24 Apr 1998

Emsley J, Cruz M, Handin R, Liddington R

Abstract excerpt

von Willebrand Factor (vWF) is a multimeric protein that mediates platelet adhesion to exposed subendothelium at sites of vascular injury under conditions of high flow/shear. The A1 domain of vWF (vWF-A1) forms the principal binding site for platelet glycoprotein Ib (GpIb), an interaction that is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Crystallography, X-Ray
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Recombinant Proteins

Share to von Willebrand Factor

Source

Identifiers

PMID: 9553097
DOI: 10.1074/jbc.273.17.10396

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9553097-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib.PMID 9553097Read ↗

Structural basis of von Willebrand factor activation by the snake toxin botrocetin.Semantic proximity Read ↗

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

Structure and function of the von Willebrand factor A1 domain.Semantic proximity Read ↗

Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations.Semantic proximity Read ↗

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

Molecular mechanism and classification of von Willebrand disease.Semantic proximity Read ↗

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

Type 2B von Willebrand disease mutations differentially perturb autoinhibition of the A1 domain.Semantic proximity Read ↗

Structure and function of von Willebrand factorSemantic proximity Read ↗

New concepts in von Willebrand disease.Semantic proximity Read ↗

ON THE VERSATILITY OF VON WILLEBRAND FACTORSemantic proximity Read ↗

Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.