ArticleJournal of enzyme inhibition and medicinal chemistry2017
Probing the druggability of membrane-bound Rab5 by molecular dynamics simulations.
Article in Journal of enzyme inhibition and medicinal chemistry, 2017. 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, 16 citations in OpenAlex.
- Drug Repurposing for Kala-Azar.Pharmaceutics · 2025Article
- Article
- Endocytosis in the context-dependent regulation of individual and collective cell properties.Nature reviews. Molecular cell biology · 2021Review
- Molecular Dynamics Simulation of Lipid-Modified Signaling Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- P38α MAPK Signaling-A Robust Therapeutic Target for Rab5-Mediated Neurodegenerative Disease.International journal of molecular sciences · 2020Review
- Article
- Structure and Dynamics of Mono- vs. Doubly Lipidated Rab5 in Membranes.International journal of molecular sciences · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Recognition and stabilization of geranylgeranylated human Rab5 by the GDP Dissociation Inhibitor (GDI).Small GTPases · 2019Article
- Structural and Biophysical Characterization of Rab5a from Leishmania Donovani.Biophysical journal · 2018Article
- Reconstitution of membrane tethering mediated by Rab-family small GTPases.Biophysical reviews · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rab5 is a small GTPase and a key regulator in early endosomal trafficking. Rab5 and its effectors are involved in a large number of infectious diseases and certain types of cancer. We performed µs atomistic molecular dynamics simulations of inactive and active full-length Rab5 anchored to a complex model bilayer with composition of the early endosome membrane. Direct interactions between the Rab5 G domain and the bilayer were observed. We found two dominant nucleotide-dependent orientations characterised by a different accessibility of the switch regions. The "buried switch" orientation was mainly associated with inactive Rab5 accompanied with a rather extended structure of the hypervariable C-terminal region. Active Rab5 preferred an orientation in which the switch regions are accessible to effector proteins. These structural differences may provide an opportunity to selectively target one Rab5 state and lead to new approaches in the development of Rab5-specific therapies.
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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.