Oligomerisation mediated by the D2 domain of DTX3L is critical for DTX3L-PARP9 reading function of mono-ADP-ribosylated androgen receptor.

Vela-Rodríguez C, Yang C, Alanen HI, Eki R, Abbas TA, Maksimainen MM, Glumoff T, Duman R, Wagner A, Paschal BM, Lehtiö L, bioRxiv (2023) Europe PMC

SASDTN5 – The D2 domain of E3 ubiquitin-protein ligase DTX3L (I101-Q200)

E3 ubiquitin-protein ligase DTX3L
MWexperimental 42 kDa
MWexpected 46 kDa
VPorod 91 nm3
log I(s) 1.23×10-1 1.23×10-2 1.23×10-3 1.23×10-4
E3 ubiquitin-protein ligase DTX3L small angle scattering data  s, nm-1
ln I(s)
E3 ubiquitin-protein ligase DTX3L Guinier plot ln 1.23×10-1 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
E3 ubiquitin-protein ligase DTX3L Kratky plot 1.104 0 3 sRg
Dmax: 112 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the D2 domain of E3 ubiquitin-protein ligase DTX3L in 30 mM HEPES, 350 mM NaCl, 5% (v/v) glycerol, 0.5 mM TCEP, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 56.00 μl sample at 10 mg/ml was injected at a 0.06 ml/min flow rate onto a GE Superose 6 Increase 3.2/300 column at 4°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

CAUTION: Data are truncated at low-s (limited low-angle/Guinier region). Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

E3 ubiquitin-protein ligase DTX3L (DTX3L)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   11.6 kDa
 
UniProt   Q8TDB6 (101-200)
Sequence   FASTA