Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs.

Martínez-Lumbreras S, Träger LK, Mulorz MM, Payr M, Dikaya V, Hipp C, König J, Sattler M, Nat Commun 15(1):3888 (2024) Europe PMC

SASDSK7 – Tandem of WW domains of Pre-mRNA-processing factor 40 homolog A (PRPF40A)

Pre-mRNA-processing factor 40 homolog A
MWexperimental 11 kDa
MWexpected 11 kDa
VPorod 17 nm3
log I(s) 6.07×100 6.07×10-1 6.07×10-2 6.07×10-3
Pre-mRNA-processing factor 40 homolog A small angle scattering data  s, nm-1
ln I(s)
Pre-mRNA-processing factor 40 homolog A Guinier plot ln 6.07×100 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Pre-mRNA-processing factor 40 homolog A Kratky plot 1.104 0 3 sRg
p(r)
Pre-mRNA-processing factor 40 homolog A pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.4 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the tandem WW domains of PRPF40A in 20 mM sodium phosphate, 100 mM NaCl, 0.5 mM DTT, pH 6.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099186 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 50.00 μl sample at 6 mg/ml was injected at a 0.16 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 25°C. 35 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Pre-mRNA-processing factor 40 homolog A (PRPF40A)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   11.4 kDa
 
UniProt   O75400 (141-236)
Sequence   FASTA