Allosteric signaling in protein kinases is an attractive target for a wide circle of molecular biologists and drug developers. Multiple methods that allow researchers to probe the transmission of the signal have been developed in recent years. These methods, however, fail to reach a consensus on which  residues constitute the “allosteric pathways” responsible for the allosteric regulation even in cases of very simple and well studied proteins. An alternative view suggests that allosteric signaling should not be associated with any contiguous allosteric pathways. Instead, it can be a result of changes in dynamics of the whole protein. This model of allostery is rooted in the extensively used model of protein molecules as ensembles of coupled oscillators. The most recent advances in studies of synchronization in dynamic systems, together with the well established fractal-like distribution of contacts in proteins, create an opportunity to combine all these features in an atomistic model of allostery. Implementation of these principles for protein kinase A are discussed.<br/>

In pursuit of elusive allosteric pathways in protein kinases

2019 Fall National Meeting

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