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Article

Mechanistic insights from a refined three-dimensional model of integrin alphaIIbbeta3.

The Journal of biological chemistry - 4 Jun 2004

Filizola Marta, Hassan Sergio A, Artoni Andrea, Coller Barry S, Weinstein Harel

Abstract excerpt

The integrin alpha(IIb)beta(3) plays an important role in platelet function, and abnormalities of this protein result in a serious bleeding disorder, known as Glanzmann thrombasthenia. Although crystallographic data exist for the related integrin alpha(V)beta(3), to date, there are no high resolution structures of integrin alpha(IIb)beta(3) available in the literature. Therefore, it is still unclear how specific...

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Identifiers

PMID: 15056669
DOI: 10.1074/jbc.M400243200

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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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Mechanistic insights from a refined three-dimensional model of integrin alphaIIbbeta3.PMID 15056669Read ↗

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A two-amino acid insertion in the Cys146- Cys167 loop of the alphaIIb subunit is associated with a variant of Glanzmann thrombasthenia. Critical role of Asp163 in ligand binding.Semantic proximity Read ↗

A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.Semantic proximity Read ↗

A Leu117-->Trp mutation within the RGD-peptide cross-linking region of beta3 results in Glanzmann thrombasthenia by preventing alphaIIb beta3 export to the platelet surface.Semantic proximity Read ↗

Molecular dynamics simulations involving different β-propeller mutations reported in Swiss and French patients correlate with their disease phenotypes.Semantic proximity Read ↗

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