I am interested in stabilizing a protein that has a low affinity tetramer by fusing the monomers to a protein domain with a high propensity for tetramerization. The protein of interest is a dimer of heterodimers, so a tetramerization domain of similar make would be ideal to form the correct assembly of the protein of interest. Can anyone recommend a small domain that forms a high affinity tetramer of this nature (dimer of heterodimers) and is amenable to being fused to a larger domain?
Hi Nichole,
I am not sure what size of protein you want to use but you can go for GAPDH. It is well characterized and so you will get all the essential information required to plan your experiment. Otherwise you can use tetramerizing fluorescent proteins as well. Good luck with your experiment.
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Best,
Kalpana
Maybe this one will help?http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2708066/pdf/pro0018-0329.pdf
However, this synthetic domain was fused to polypeptides only.
Best,
Vladimir
Why not a coiled-coil? That's what coiled-coil oligomerization domains do. I would guess any tetrameric coiled coil would work.
Here is one example of the approach but for trimers:
http://www.ncbi.nlm.nih.gov/pubmed/18093992
For dimer of heterodimers one of these might work:
http://www.sciencedirect.com/science/article/pii/S1074552108002743
http://pubs.acs.org/doi/abs/10.1021/bi060092q
There should be also tetrameric coiled coils maybe even GCN4 derivatives but be aware to use a proper spacer between coiled coil and your protein.
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