I would like to ask whether there is any method/way to bind to a protein like FAK (not FAT and DERM domains but the kinase) without affecting its function?
Such as using DNA/RNA/peptide sequence?
I hardly search out relevant literature reporting this
Binding to the NES2 sequence may be a good way. But this seems a universal NES sequence in homosapiens
The versatile structure of FAK increases the number of additional binding partners that interact with FAK via indirect or secondary interactions. The identification of the interactome of FAK is required to understand the regulation of this oncogene and target new binding partners as potential therapeutics for cancer. The MS-based methods can be combined with a wide range of protein purification and protein capture strategies, such as immunoprecipitation, thus allowing rapid and reliable identification of components.
I am not sure what is your experimental requirement for such binding. Binding of any bio-molecule to kinase domain have a good chance to interrupt in function. If you just want to bind some molecule for detection/localization/interaction purpose you can always use a tagged protein overexpression/crisper edit in c-terminal of such protein.
Nandini Verma Thanks for your answer Nandini. What if we just bind to non-functional position of the kinase? I would like to design a probe based on binding to the kinase domain
Overpressing/gene editing a fluorescent protein tag to it is the strategy i don't want.
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