Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites.

Simon B, Huart AS, Temmerman K, Vahokoski J, Mertens HD, Komadina D, Hoffmann JE, Yumerefendi H, Svergun DI, Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M, Structure 24(6):851-61 (2016) Europe PMC

SASDB62 – Death associated protein kinase (D220K mutant)

Death associated protein kinase (D220K mutant)
MWexperimental 37 kDa
MWexpected 37 kDa
VPorod 89 nm3
log I(s) 7.17×102 7.17×101 7.17×100 7.17×10-1
Death associated protein kinase (D220K mutant) small angle scattering data  s, nm-1
ln I(s)
Death associated protein kinase (D220K mutant) Guinier plot ln 7.17×102 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Death associated protein kinase (D220K mutant) Kratky plot 1.104 0 √3 sRg
p(r)
Death associated protein kinase (D220K mutant) pair distance distribution function Rg: 2.6 nm 0 Dmax: 9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Death associated protein kinase (D220K mutant) NONE model
Death associated protein kinase (D220K mutant) NONE model
Synchrotron SAXS data from solutions of Death associated protein kinase (D220K mutant) in 50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol, 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 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 10°C. 20 successive 0.050 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.

Characterisation of effect of mutation D220K of hDAPK2 on dimer formation

Death associated protein kinase (D220K mutant) (hDAPK2 D220K)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Other
Mon. MW   37.3 kDa
Sequence   FASTA