ArticleThe Journal of biological chemistry2009
Localizing the membrane binding region of Group VIA Ca2+-independent phospholipase A2 using peptide amide hydrogen/deuterium exchange mass spectrometry.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The trial behind it
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Who cites it
45 citing papers in PubMed.
- Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms.FEBS open bio · 2026Review
- Conformational Dynamics and Activation of Membrane-Associated Human Group IVA Cytosolic Phospholipase AThe journal of physical chemistry letters · 2025Article
- The mechanism of allosteric regulation of calcium-independent phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular basis of unique specificity and regulation of group VIA calcium-independent phospholipase APharmacology & therapeutics · 2023Review
- The Phospholipase A2 Superfamily: Structure, Isozymes, Catalysis, Physiologic and Pathologic Roles.International journal of molecular sciences · 2023Review
- Regulatory mechanisms triggered by enzyme interactions with lipid membrane surfaces.Frontiers in molecular biosciences · 2023Review
- Membrane Association Allosterically Regulates Phospholipase AAccounts of chemical research · 2022Article
- Cardiolipin interacts with beta-2-glycoprotein I and forms an open conformation-Mechanisms analyzed using hydrogen/deuterium exchange.Protein science : a publication of the Protein Society · 2021Article
- Unraveling cardiolipin-induced conformational change of cytochrome c through H/D exchange mass spectrometry and quartz crystal microbalance.Scientific reports · 2021Article
- Probing Protein-Membrane Interactions and Dynamics Using Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS).Methods in molecular biology (Clifton, N.J.) · 2021Article
- Characterization of the ExoU activation mechanism using EPR and integrative modeling.Scientific reports · 2020Article
- Phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
- Dynamic structural biology at the protein membrane interface.The Journal of biological chemistry · 2019Review
- Article
- Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.Journal of the American Chemical Society · 2018Article
- The structure of iPLANature communications · 2018Article
- Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry.The Journal of biological chemistry · 2017Article
- Analyses of Calcium-Independent Phospholipase AMethods in enzymology · 2017Article
- Liberating Chiral Lipid Mediators, Inflammatory Enzymes, and LIPID MAPS from Biological Grease.The Journal of biological chemistry · 2016Review
- Computer-aided drug design guided by hydrogen/deuterium exchange mass spectrometry: A powerful combination for the development of potent and selective inhibitors of Group VIA calcium-independent phospholipase ABioorganic & medicinal chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The Group VIA-2 Ca(2+)-independent phospholipase A(2) (GVIA-2 iPLA(2)) is composed of seven consecutive N-terminal ankyrin repeats, a linker region, and a C-terminal phospholipase catalytic domain. No structural information exists for this enzyme, and no information is known about the membrane binding surface. We carried out deuterium exchange experiments with the GVIA-2 iPLA(2) in the presence of both phospholipid substrate and the covalent inhibitor methyl arachidonoyl fluorophosphonate and located regions in the protein that change upon lipid binding. No changes were seen in the presence of only methyl arachidonoyl fluorophosphonate. The region with the greatest change upon lipid binding was region 708-730, which showed a >70% decrease in deuteration levels at numerous time points. No decreases in exchange due to phospholipid binding were seen in the ankyrin repeat domain of the protein. To locate regions with changes in exchange on the enzyme, we constructed a computational homology model based on homologous structures. This model was validated by comparing the deuterium exchange results with the predicted structure. Our model combined with the deuterium exchange results in the presence of lipid substrate have allowed us to propose the first structural model of GVIA-2 iPLA(2) as well as the interfacial lipid binding region.
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Registered trials
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