ArticlePloS one2013
A single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Aging-associated changes in immunological parameters: Implications for COVID-19 immune response in the elderly.Physiological reports · 2025Review
- Simulation of gap junction formation reveals critical role of Cys disulfide redox state in connexin hemichannel docking.Cell communication and signaling : CCS · 2024Article
- Exogenous Integrin αIIbβ3 Inhibitors Revisited: Past, Present and Future Applications.International journal of molecular sciences · 2021Review
- Extracellular Redox Regulation of α7β Integrin-Mediated Cell Migration Is Signaled via a Dominant Thiol-Switch.Antioxidants (Basel, Switzerland) · 2020Article
- Investigation and Prediction of Human Interactome Based on Quantitative Features.Frontiers in bioengineering and biotechnology · 2020Article
- Platelet Function in Aging.Frontiers in cardiovascular medicine · 2019Review
- Accessibility explains preferred thiol-disulfide isomerization in a protein domain.Scientific reports · 2017Article
- αIIbβ3 variants defined by next-generation sequencing: predicting variants likely to cause Glanzmann thrombasthenia.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamics.Current pharmaceutical design · 2015Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The integrins are a family of membrane receptors that attach a cell to its surrounding and play a crucial function in cell signaling. The combination of internal and external stimuli alters a folded non-active state of these proteins to an extended active configuration. The β3 subunit of the platelet αIIbβ3 integrin is made of well-structured domains rich in disulfide bonds. During the activation process some of the disulfides are re-shuffled by a mechanism requiring partial reduction of some of these bonds; any disruption in this mechanism can lead to inherent blood clotting diseases. In the present study we employed Molecular Dynamics simulations for tracing the sequence of structural fluctuations initiated by a single cysteine mutation in the β3 subunit of the receptor. These simulations showed that in-silico protein mutants exhibit major conformational deformations leading to possible disulfide exchange reactions. We suggest that any mutation that prevents Cys560 from reacting with one of the Cys(567)-Cys(581) bonded pair, thus disrupting its ability to participate in a disulfide exchange reaction, will damage the activation mechanism of the integrin. This suggestion is in full agreement with previously published experiments. Furthermore, we suggest that rearrangement of disulfide bonds could be a part of a natural cascade of thiol/disulfide exchange reactions in the αIIbβ3 integrin, which are essential for the native activation process.
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