There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
There are no known binding partners that would interact with the periplasmic domain of AmtB.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
Additionally, it is likely that there are other binding partners that vary with cell type and environmental conditions.
We identified p33ING1 as a binding partner that interacts with CSIG.
The open structure of disordered assemblers is largely preserved upon scaffolding their partner proteins, resulting in a large binding interface that enables multiple proteins to be bound by a single IDR.
In this case, almost trivially, the finding of the binding partners is enabled by a non-specific element encoded in their respective structures – the hydrophobicity of their overall molecular surface.
Phosphorylation can affect protein protein interactions (PPIs), abolishing interaction with previous binding partners or enabling new interactions.
The large number of additional, lateral binding sites sometimes creates large cooperativity effects that enable filaments to bind with extreme affinity to their partner, even if the individual binding energies, per subunit, are rather small.
