ArticlePLoS computational biology2019
Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations.
Article in PLoS computational biology, 2019. 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.
- Mechanisms driving open-closed transitions and dimer stability of the large GTPases hGBP1 and hGBP5.Frontiers in molecular biosciences · 2026Article
- OPA1 mutations in dominant optic atrophy: domain-specific defects in mitochondrial fusion and apoptotic regulation.Journal of translational medicine · 2025Article
- Revealing innovative JAK1 and JAK3 inhibitors: a comprehensive study utilizing QSAR, 3D-Pharmacophore screening, molecular docking, molecular dynamics, and MM/GBSA analyses.Frontiers in molecular biosciences · 2024Article
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- Guanylate-Binding Protein 2 Exerts GTPase-Dependent Anti-Ectromelia Virus Effect.Microorganisms · 2023Article
- Article
- The large GTPase AtGBPL3 links nuclear envelope formation and morphogenesis to transcriptional repression.Nature plants · 2023Article
- Domain motions, dimerization, and membrane interactions of the murine guanylate binding protein 2.Scientific reports · 2023Article
- Toxoplasma-proximal and distal control by GBPs in human macrophages.Pathogens and disease · 2022Article
- Exploring Large Domain Motions in Proteins Using Atomistic Molecular Dynamics with Enhanced Conformational Sampling.International journal of molecular sciences · 2020Article
- Guanylate-Binding Protein 1: An Emerging Target in Inflammation and Cancer.Frontiers in immunology · 2019Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Guanylate binding proteins (GBPs) belong to the dynamin-related superfamily and exhibit various functions in the fight against infections. The functions of the human guanylate binding protein 1 (hGBP1) are tightly coupled to GTP hydrolysis and dimerization. Despite known crystal structures of the hGBP1 monomer and GTPase domain dimer, little is known about the dynamics of hGBP1. To gain a mechanistic understanding of hGBP1, we performed sub-millisecond multi-resolution molecular dynamics simulations of both the hGBP1 monomer and dimer. We found that hGBP1 is a highly flexible protein that undergoes a hinge motion similar to the movements observed for other dynamin-like proteins. Another large-scale motion was observed for the C-terminal helix α13, providing a molecular view for the α13-α13 distances previously reported for the hGBP1 dimer. Most of the loops of the GTPase domain were found to be flexible, revealing why GTP binding is needed for hGBP1 dimerization to occur.
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