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These mutations may impair protein function by altering the catalytic activity, the propensity to bind to physiological partners, as well as by affecting steady-state levels (by modifying protein expression or stability).
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In some cases, such as the Grb2 adapter protein GrpL or the phosphodiesterase PDE4A5, an SH3-domain within the substrate is removed causing its inability to bind to physiological interaction partners.
However, it has proven very difficult to globally test whether structured hubs bind to disordered partners.
As these conformations bind to their partners, they are removed from the pool of free protein.
It is thus uncertain if rice Hbs bind to other partners.
While numerous papers suggest that flexibility could enable one protein to bind to many partners, we might have been the first to suggest that flexibility would provide a means for multiple sequences to bind to a common partner.
The ability of a protein to bind to multiple partners was suggested to involve new principles [ 26].
Chameleon behavior could be an important feature that enables one disordered region to bind to multiple partners.
What if a region used to bind to multiple partners uses different secondary structures and different amino acids?
That is, it uses the same or similar face of its globular structure to bind to multiple partners.
These proteins can bind the same partner in different conformations or bind to completely different partners through the disordered binding regions [ 122].
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