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Recent studies have highlighted the importance, however, of changes in protein flexibility as an effective way to mediate allosteric communication across a protein.
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Together with the identification of hotspot residues acting as mediators of allosteric communication, our data provide a glimpse into the dynamic spectrum of iGluRs.
Allosteric communication underlies ligand-dependent transcriptional responses mediated by nuclear receptors.
The mechanism of this allosteric communication remains largely unexplored.
Protein dynamics is the basis for allosteric communication.
Moreover, averages of local mechanical properties can be used to identify long-range couplings between sites (i.e., allosteric communication).
The function of GroE requires a complex system of allosteric communication driven by protein nucleotide interactions.
Our results suggest that the H10 helix and specifically W229 are important modulators of the allosteric communication between the active site and the allosteric site.
Our observations suggest that metal-binding sites may have been evolutionary selected to achieve optimum allosteric communication.
In this review we describe the current state of the computational methods that provide insights into the allosteric communication in GPCRs and elucidate how this information can be used to design allosteric modulators.
Inter-ring allosteric communication thus appears indispensable for the function of GroEL, and an engineered single-ring version (SR1) cannot substitute for GroEL in vivo.
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