Structural basis of ubiquitin ligase Nedd4-2 autoinhibition and regulation by calcium and 14-3-3 proteins

Janosev M, Kosek D, Tekel A, Joshi R, Honzejkova K, Pohl P, Obsil T, Obsilova V
Nature Communications 16(1) (2025 May 26)

doi: 10.1038/s41467-025-60207-4 		Submitted to SASBDB: 2025 Feb 20
Published in SASBDB:

SASDUC3 – Phosphorylated E3 ubiquitin-protein ligase Nedd4-2 in the absence of calcium

Isoform 5 of E3 ubiquitin-protein ligase NEDD4-like experimental SAS data
CORAL model
Sample: Isoform 5 of E3 ubiquitin-protein ligase NEDD4-like monomer, 110 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 1 mM EDTA, 3% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Aug 17
RgGuinier 4.9 nm
Dmax 22.0 nm
VolumePorod 206 nm3

SASDUD3 – Phosphorylated E3 ubiquitin-protein ligase Nedd4-2 in the presence of calcium

Isoform 5 of E3 ubiquitin-protein ligase NEDD4-like experimental SAS data
Isoform 5 of E3 ubiquitin-protein ligase NEDD4-like Kratky plot
Sample: Isoform 5 of E3 ubiquitin-protein ligase NEDD4-like monomer, 110 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 1 mM CaCl2, 3% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Aug 17
RgGuinier 4.9 nm
Dmax 22.5 nm
VolumePorod 201 nm3