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