Dynamic activation of an allosteric regulatory protein

Shiou-Ru Tzeng and Charalampos G. Kalodimos ()
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Shiou-Ru Tzeng: Department of Chemistry & Chemical Biology,
Charalampos G. Kalodimos: Department of Chemistry & Chemical Biology,

Nature, 2009, vol. 462, issue 7271, 368-372

Abstract: Allostery goes dynamic Effector molecules are thought to control the activity of allosteric proteins by binding to an allosteric site, distinct from the active site, thereby inducing and stabilizing a specific conformational state of the protein. A new study suggests that the notion of purely structurally regulated activity in allosteric proteins should be revised to include a frequently dominating contribution from protein dynamics. Shiou-Ru Tzeng and Charalampos Kalodimos characterized cyclic AMP binding to catabolite activator protein (CAP), a transcriptional activator often used as a model for allostery. They find, surprisingly, that even when in a structurally inactive conformation, CAP can be activated for ligand (DNA) binding by changes in protein dynamics.

Date: 2009
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DOI: 10.1038/nature08560

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