ArticleBiophysical journal2008
Interactions between neuronal fusion proteins explored by molecular dynamics.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- From complex data to clear insights: visualizing molecular dynamics trajectories.Frontiers in bioinformatics · 2024Review
- Review
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex.Biophysical journal · 2018Article
- A membrane-inserted structural model of the yeast mitofusin Fzo1.Scientific reports · 2017Article
- The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex.PloS one · 2017Article
- Interaction of the Complexin Accessory Helix with Synaptobrevin Regulates Spontaneous Fusion.Biophysical journal · 2016Article
- Role of Internal Water on Protein Thermal Stability: The Case of Homologous G Domains.The journal of physical chemistry. B · 2015Article
- Coarse-Grained Model of SNARE-Mediated Docking.Biophysical journal · 2015Article
- Interaction of the complexin accessory helix with the C-terminus of the SNARE complex: molecular-dynamics model of the fusion clamp.Biophysical journal · 2013Article
- Is assembly of the SNARE complex enough to fuel membrane fusion?The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this report, we present features of the neuronal SNARE complex determined by atomistic molecular dynamics simulations. The results are robust for three models, varying force fields (AMBER and GROMOS) and solvent environment (explicit and implicit). An excellent agreement with experimental findings is observed. The SNARE core complex behaves like a stiff rod, with limited conformational dynamics. An accurate picture of the interactions within the complex emerges with a characteristic pattern of atomic contacts, hydrogen bonds, and salt bridges reinforcing the underlying layer structure. This supports the metaphor of a molecular Velcro strip that has been used by others to describe the neuronal fusion complex. No evidence for directionality in the formation of these interactions was found. Electrostatics largely dominates all interactions, with an acidic surface patch structuring the hydration layers surrounding the complex. The interactions within the four-helix bundle are asymmetric, with the synaptobrevin R-SNARE notably exhibiting an increased rigidity with respect to the three Q-SNARE helices. The interaction patterns we observe provide a new tool for interpreting the impact of mutations on the complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.