Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 37, Issue -, Pages 1-8Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.10.004
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The presence of multiple allosteric sites in proteins motivates development of allosteric drugs modulators of protein activity with potentially higher specificity and less toxicity than traditional orthosteric compounds. A quest for allosteric control of any protein starts from the identification and characterization of allosteric sites. Protein dynamics is the basis for allosteric communication. Binding of effector molecules to allosteric sites modulates structural dynamics, thus affecting activity of remote functional sites. We review here theoretical concepts and experimental approaches for exploring allosteric sites, their role in allosteric regulation, and ways to assess their druggability. Key steps of the design procedure aimed at obtaining allosteric drugs with required agonistic/antagonistic effect are proposed, and their computational and experimental elements are discussed.
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