ArticleJournal of molecular modeling2016
Molecular insights into the binding of phosphoinositides to the TH domain region of TIPE proteins.
Article in Journal of molecular modeling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Lipid transfer proteins and instructive regulation of lipid kinase activities: Implications for inositol lipid signaling and disease.Advances in biological regulation · 2020Review
- Regulatory Roles of Tumor Necrosis Factor-α-Induced Protein 8 Like-Protein 2 in Inflammation, Immunity and Cancers: A Review.Cancer management and research · 2020Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- TNFAIP8: Inflammation, Immunity and Human Diseases.Journal of cellular immunology · 2019Article
- Structural basis of Gip1 for cytosolic sequestration of G protein in wide-range chemotaxis.Nature communications · 2018Article
- TIPE Family of Proteins and Its Implications in Different Chronic Diseases.International journal of molecular sciences · 2018Review
- Crosslink between lipids and acute uveitis: a lipidomic analysis.International journal of ophthalmology · 2018Article
- TIPE3 in Cancer: A Multifaceted Regulator of Tumorigenesis, Therapeutic Resistance, and Clinical Outcomes.Technology in cancer research & treatmentReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatidylinositols and their phosphorylated derivatives, phosphoinositides, play a central role in regulating diverse cellular functions. These phospholipids have been shown to interact with the hydrophobic TH domain of the tumor necrosis factor (TNF)-α-induced protein 8 (TIPE) family of proteins. However, the precise mechanism of interaction of these lipids is unclear. Here we report the binding mode and interactions of these phospholipids in the TH domain, as elucidated using molecular docking and simulations. Results indicate that phosphoinositides bind to the TH domain in a similar way by inserting their lipid tails in the hydrophobic cavity. The exposed head group is stabilized by interactions with critical positively charged residues on the surface of these proteins. Further MD simulations confirmed the dynamic stability of these lipids in the TH domain. This computational analysis thus provides insight into the binding mode of phospholipids in the TH domain of the TIPE family of proteins. Graphical abstract A phosphoinositide (phosphatidylinositol 4-phosphate; PtdIns4P) docked to TIPE2.
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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.