ArticleBiochemistry2019
Modulating Integrin αIIbβ3 Activity through Mutagenesis of Allosterically Regulated Intersubunit Contacts.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Conformational response of αStructure (London, England : 1993) · 2025Article
- Elucidation of the molecular interactions that enable stable assembly and structural diversity in multicomponent immune receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single point mutations can potentially enhance infectivity of SARS-CoV-2 revealed byRSC advances · 2021Article
- Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site.Journal of the American Chemical Society · 2021Article
- Association Between Low-Density Lipoprotein Cholesterol and Platelet Distribution Width in Acute Ischemic Stroke.Frontiers in neurology · 2021Article
- A defined structural unit enables de novo design of small-molecule-binding proteins.Science (New York, N.Y.) · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
Integrin αIIbβ3, a transmembrane heterodimer, mediates platelet aggregation when it switches from an inactive to an active ligand-binding conformation following platelet stimulation. Central to regulating αIIbβ3 activity is the interaction between the αIIb and β3 extracellular stalks, which form a tight heterodimer in the inactive state and dissociate in the active state. Here, we demonstrate that alanine replacements of sensitive positions in the heterodimer stalk interface destabilize the inactive conformation sufficiently to cause constitutive αIIbβ3 activation. To determine the structural basis for this effect, we performed a structural bioinformatics analysis and found that perturbing intersubunit contacts with favorable interaction geometry through substitutions to alanine quantitatively accounted for the degree of constitutive αIIbβ3 activation. This mutational study directly assesses the relationship between favorable interaction geometry at mutation-sensitive positions and the functional activity of those mutants, giving rise to a simple model that highlights the importance of interaction geometry in contributing to the stability between protein-protein interactions.
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