| MWexperimental | 15 | kDa |
| MWexpected | 15 | kDa |
| VPorod | 27 | nm3 |
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log I(s)
2.39×10-2
2.39×10-3
2.39×10-4
2.39×10-5
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s, nm-1
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Targeting the phosphoprotein enriched in diabetes/astrocytes 15 death effector domain via fragment-based and integrative structural biology approaches.
Mercurio I, Carucci F, Nanna V, Di Marino S, Papadopoulos MGE, Bischetti M, Fata F, Malgieri G, Siliqi D Piai A, Fattorusso R, Mangiatordi GF, Toniatti C, Saviano M, Alberga D, Int J Biol Macromol :154849 (2026) Europe PMCSASDX35 – DD mutant astrocytic phosphoprotein PEA-15
Astrocytic phosphoprotein PEA-15 (S104D, S116D)|
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Fits and models
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Synchrotron SAXS data from solutions of PEA15-DD mutant, in 20 mM Na2PO4 2mM DTT pH=7.0 were collected on the P12 beamline at DESY (Hamburg, Germany) using a Pilatus 6m detector at a sample-detector distance of 3.0 m and a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). A solute concentration of 0.6 to 2.2 mg/ml was measured at 20°C. 20 successive 0.1-second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged and brought into the absolute scale with respect to the intensity of the empty capillary and the water; the scattering of the solvent-blank was subtracted. First, a Ca model was reconstructed by GASBOR which fits quite well with the NMR model (PDB ID 1N3K). Second, the long C-tail was added to the NMR model as dummy-residues, where the spatial position of the tail was optimised using the program CORAL.The goal of SAXS data was to assess differences in the spatial sampling/conformation of the DD mutant variant compared to the wild-type protein.
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