Making the invisible visible: Toward structural characterization of allosteric states,interaction networks,and allosteric regulatory mechanisms in protein kinases |
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| Institution: | 1. Keck Center for Science and Engineering, Schmid College of Science and Technology, Chapman University, One University Drive, Orange, CA, 92866, USA;2. Department of Biomedical and Pharmaceutical Sciences, Chapman University School of Pharmacy, 9401 Jeronimo Road, Irvine, CA, 92618, USA;1. Department of Pharmacology, University of California at San Diego, La Jolla, CA, 92093, USA;2. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA, 92093, USA;1. Department of Biological Sciences, National University of Singapore, Singapore;2. Instituto de Investigación en Biomedicina de Buenos Aires - CONICET - Partner Institute of the Max Planck Society, Buenos Aires, Argentina;3. Bioinformatics Institute, Agency for Science, Technology and Research, Matrix, Singapore |
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| Abstract: | Despite the established view of protein kinases as dynamic and versatile allosteric regulatory machines, our knowledge of allosteric functional states, allosteric interaction networks, and the intrinsic folding energy landscapes is surprisingly limited. We discuss the latest developments in structural characterization of allosteric molecular events underlying protein kinase dynamics and functions using structural, biophysical, and computational biology approaches. The recent studies highlighted progress in making the invisible aspects of protein kinase ‘life’ visible, including the determination of hidden allosteric states and mapping of allosteric energy landscapes, discovery of new mechanisms underlying ligand-induced modulation of allosteric activity, evolutionary adaptation of kinase allostery, and characterization of allosteric interaction networks as the intrinsic driver of kinase adaptability and signal transmission in the regulatory assemblies. |
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