1 reply to this topic

[joek1]

I have a protein which binds Src under non-stimulated conditions, upon EGF stimulation there appears to be a dissociation between the protein and Src. Mass Spec phosphorylation data shows an EGF-stimulated phospho site in a proline rich region which may contain a potential Src SH3 binding site. How could I determine if the phosphorylation site is responsible for the dissociation from Src?
Thanks.

[Simonsays]

Hi!
I'd try directed mutagenesis of the residue for a glycine or an alanine... Express your protein and see if Src is still able to bind it under basal conditions

How about it?

Simon