ArticleInternational journal of molecular sciences2024
Identifying Residues for Substrate Recognition in Human GPAT4 by Molecular Dynamics Simulations.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 2 citations in OpenAlex.
- GPAT4 regulates antitumor immune response through activating the mtDNA-cGAS axis in cancer cells.Cell insight · 2026Article
- Protein-Ligand Interactions: Recent Advances in Biophysics, Biochemistry, and Bioinformatics.International journal of molecular sciences · 2025Article
- CHP1 promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the first step in triacylglycerol synthesis. Understanding its substrate recognition mechanism may help to design drugs to regulate the production of glycerol lipids in cells. In this work, we investigate how the native substrate, glycerol-3-phosphate (G3P), and palmitoyl-coenzyme A (CoA) bind to the human GPAT isoform GPAT4 via molecular dynamics simulations (MD). As no experimentally resolved GPAT4 structure is available, the AlphaFold model is employed to construct the GPAT4-substrate complex model. Using another isoform, GPAT1, we demonstrate that once the ligand binding is properly addressed, the AlphaFold complex model can deliver similar results to the experimentally resolved structure in MD simulations. Following the validated protocol of complex construction, we perform MD simulations using the GPAT4-substrate complex. Our simulations reveal that R427 is an important residue in recognizing G3P via a stable salt bridge, but its motion can bring the ligand to different binding hotspots on GPAT4. Such high flexibility can be attributed to the flexible region that exists only on GPAT4 and not on GPAT1. Our study reveals the substrate recognition mechanism of GPAT4 and hence paves the way towards designing GPAT4 inhibitors.
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Registered trials
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