Sos-Binding

Reaction

$inactiveSos + activeEGFR \rightleftharpoons activeSos$

Rate Equation

$v_{Sos-binding} = k_{Sos-binding} \cdot [activeEGFR][inactiveSos] - k_{Sos-release} \cdot [activeSos]$

final Parameter

The errors of the final parameter are increased by 50% because only a similar reaction is modelled.

$k_{Sos-binding}= 1.47 \cdot 10^8 \pm 1.83 \cdot 10^8 \cdot 1.5\ \frac{1}{M \cdot s} = 1.47 \cdot 10^2 \pm 2.745 \cdot 10^2\ \frac{1}{\mu M \cdot s}$
$k_{Sos-release} = 0.16 \pm 1.81 \cdot 10^{-2} \cdot 1.5\ \frac{1}{s} = 0.16 \pm 2.715 \cdot 10^{-2}\ \frac{1}{s}$

Parameter

Parameter	Notes	References
$k_{Sos-association}= 3.34 * 10^6\ \frac{1}{\mu Ms}$ $k_{Sos-release}= 0.14\ \frac{1}{s}$ $K_D = 42\ nM$	The binding of the p85αSH2-N domain to 17-mer phosphopeptide similar to a PDGFR region. M. Hensmann et al. "Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI3'-kinase: a heteronuclear NMR study." eng. In: Protein Sci 3.7 (1994), pp. 1020-1030. DOI: 10.1002/pro.5560030704. URL: http://dx.doi.org/10.1002/pro.5560030704
	The binding of the two different SH2 domains to phosphotyrosine containing peptides derived from and insuline receptor substrate.	S. Felder et al. "SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange." eng. In Mol Cell Biol 13.3 (1993), pp. 1449-1455