Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase.

Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O, Nat Commun 8(1):2101 (2017) Europe PMC

SASDC36 – DH - Dbl-homology domain of Bcr-Abl tyrosine kinase p210

BCR-ABL p210 fusion protein
MWI(0) 25 kDa
MWexpected 25 kDa
VPorod 38 nm3
log I(s) 3.73×103 3.73×102 3.73×101 3.73×100
BCR-ABL p210 fusion protein small angle scattering data  s, nm-1
ln I(s)
BCR-ABL p210 fusion protein Guinier plot ln 3.74×103 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
BCR-ABL p210 fusion protein Kratky plot 1.104 0 √3 sRg
p(r)
BCR-ABL p210 fusion protein pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
BCR-ABL p210 fusion protein PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
BCR-ABL p210 fusion protein SREFLEX model
Synchrotron SAXS data from solutions of DH - Dbl-homology domain of Bcr-Abl tyrosine kinase p210 in 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.20 mg/ml was measured at 20°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.

BCR-ABL p210 fusion protein
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.9 kDa
 
UniProt   P11274
Sequence   FASTA
 
PDB ID   5N6R
 
PDB ID   5N6R