Hi Users,
I have been reading on IRF3 protein which is a monomeric protein in non active state in the cytoplasm and the TBk1 and STING phosphorylate the 7 serines in the monomer and this becomes activated and dimerizes to a homodimer and then enters the nucleus.
If I have to study the key interactions between the 2 monomers which facilitate dimer stability what all procedure should I adopt?
The crystal structure of the dimer is available in RCSB.
Also I need to study why does it homodimerize and not heterodimerize with other IRFs like IRF4 IRF7...any ideas?
How to dissect this problem using computational approaches?
Any ideas will be deeply appreciated.
Thanks
Debarati
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Received on Sat Mar 16 2019 - 15:00:02 PDT
