Journal
CELL REPORTS
Volume 14, Issue 1, Pages 32-42Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.12.010
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Funding
- Howard Hughes Medical Institute
- Office of Basic Energy Sciences, Catalysis Science Program, U.S. Department of Energy [DE-FG02-05ER15699]
- NIH [GM100966-01, EY009514]
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Molecular recognition plays a central role in biology, and protein dynamics has been acknowledged to be important in this process. However, it is highly debated whether conformational changes happen before ligand binding to produce a binding-competent state (conformational selection) or are caused in response to ligand binding (induced fit). Proposals for both mechanisms in protein/protein recognition have been primarily based on structural arguments. However, the distinction between them is a question of the probabilities of going via these two opposing pathways. Here, we present a direct demonstration of exclusive conformational selection in protein/protein recognition by measuring the flux for rhodopsin kinase binding to its regulator recoverin, an important molecular recognition in the vision system. Using nuclear magnetic resonance (NMR) spectroscopy, stopped-flow kinetics, and isothermal titration calorimetry, we show that recoverin populates a minor conformation in solution that exposes a hydrophobic binding pocket responsible for binding rhodopsin kinase. Protein dynamics in free recoverin limits the overall rate of binding.
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