Conformational buffering underlies functional selection in intrinsically disordered protein regions.

González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB, Nat Struct Mol Biol (2022) Europe PMC

SASDNR6 – Retinoblastoma protein/Early E1A protein (RB-E1A) complex at 0.7 mg/ml

Retinoblastoma-associated protein
Early E1A protein
MWexperimental 64 kDa
MWexpected 54 kDa
VPorod 80 nm3
log I(s) 2.26×10-2 2.26×10-3 2.26×10-4 2.26×10-5
Retinoblastoma-associated protein Early E1A protein small angle scattering data  s, nm-1
ln I(s)
Retinoblastoma-associated protein Early E1A protein Guinier plot ln 2.26×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Retinoblastoma-associated protein Early E1A protein Kratky plot 1.104 0 3 sRg
Dmax: 10 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the RB-E1A complex in 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH 7 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.1244 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.70 mg/ml was measured at 25°C. 20 successive 0.045 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.

Retinoblastoma-associated protein (Rb)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   41.2 kDa
Sequence   FASTA
 
Early E1A protein (E1A)
Mol. type   Protein
Organism   Human adenovirus C serotype 5
Olig. state   Monomer
Mon. MW   12.7 kDa
Sequence   FASTA