ArticleBiophysical journal2005
X-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPC.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model.Scientific reports · 2023Article
- Membrane Association Allosterically Regulates Phospholipase AAccounts of chemical research · 2022Article
- X-ray Reflectivity Study of Polylysine Adsorption on the Surface of DMPS Monolayers.Membranes · 2022Article
- Effects of Oxygen Modification on the Structural and Magnetic Properties of Highly Epitaxial LaScientific reports · 2020Article
- Structural basis of phosphatidylcholine recognition by the C2-domain of cytosolic phospholipase AeLife · 2019Article
- Sensitivity of peripheral membrane proteins to the membrane context: A case study of phosphatidylserine and the TIM proteins.Biochimica et biophysica acta. Biomembranes · 2018Review
- Coupling X-Ray Reflectivity and In Silico Binding to Yield Dynamics of Membrane Recognition by Tim1.Biophysical journal · 2017Article
- Membrane and inhibitor interactions of intracellular phospholipases A2.Advances in biological regulation · 2016Review
- Molecular mechanism for differential recognition of membrane phosphatidylserine by the immune regulatory receptor Tim4.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The molecular basis of ceramide-1-phosphate recognition by C2 domains.Journal of lipid research · 2013Article
- Cell differentiation of pluripotent tissue sheets immobilized on supported membranes displaying cadherin-11.PloS one · 2013Article
- C2 domain membrane penetration by group IVA cytosolic phospholipase A₂ induces membrane curvature changes.Journal of lipid research · 2012Article
- NMR analyses of the interaction between the FYVE domain of early endosome antigen 1 (EEA1) and phosphoinositide embedded in a lipid bilayer.The Journal of biological chemistry · 2012Article
- Origin and correction of magnetic field inhomogeneity at the interface in biphasic NMR samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Emerging methodologies to investigate lipid-protein interactions.Integrative biology : quantitative biosciences from nano to macro · 2012Review
- Configuration of PKCalpha-C2 domain bound to mixed SOPC/SOPS lipid monolayers.Biophysical journal · 2009Article
- Modeling kinetics of subcellular disposition of chemicals.Chemical reviews · 2009Review
- Phospholipase A2 biochemistry.Cardiovascular drugs and therapy · 2009Review
- A phospholipid substrate molecule residing in the membrane surface mediates opening of the lid region in group IVA cytosolic phospholipase A2.The Journal of biological chemistry · 2008Article
- Spin-diffusion couples proton relaxation rates for proteins in exchange with a membrane interface.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors.
Funding
Abstract
X-ray reflectivity is used to study the interaction of C2 domains of cytosolic phospholipase A(2) (cPLA(2)alpha-C2) with a Langmuir monolayer of 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC) supported on a buffered aqueous solution containing Ca(2+). The reflectivity is analyzed in terms of the known crystallographic structure of cPLA(2)alpha-C2 domains and a slab model representing the lipid layer to yield an electron density profile of the lipid layer and bound C2 domains. This new method of analysis determines the angular orientation and penetration depth of the cPLA(2)alpha-C2 domains bound to the SOPC monolayer, information not available from the standard slab model analysis of x-ray reflectivity. The best-fit orientation places the protein-bound Ca(2+) ions within 1 A of the lipid phosphate group (with an accuracy of +/-3 A). Hydrophobic residues of the calcium-binding loops CBL1 and CBL3 penetrate deepest into the lipid layer, with a 2 A penetration into the tailgroup region. X-ray measurements with and without the C2 domain indicate that there is a loss of electrons in the headgroup region of the lipid monolayer upon binding of the domains. We suggest that this is due to a loss of water molecules bound to the headgroup. Control experiments with a non-calcium buffer and with domain mutants confirm that the cPLA(2)alpha-C2 binding to the SOPC monolayer is Ca(2+)-dependent and that the hydrophobic residues in the calcium-binding loops are critical for membrane binding. These results indicate that an entropic component (due to water loss) as well as electrostatic and hydrophobic interactions contributes to the binding mechanism.
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