Visualization of transient encounter complexes in protein–protein association

Chun Tang, Junji Iwahara and G. Marius Clore ()
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Chun Tang: National Institutes of Health
Junji Iwahara: National Institutes of Health
G. Marius Clore: National Institutes of Health

Nature, 2006, vol. 444, issue 7117, 383-386

Abstract: Close encounters Protein–protein interactions are involved in a large number of biological processes, and though X-ray crystallography and nuclear magnetic resonance spectroscopy can be used to examine two (or more) proteins in a complex, it is difficult to establish how the two proteins interact before they form this final complex. Tang et al. have used nuclear magnetic resonance spectroscopy to directly visualize an ensemble of transient, non-specific encounter complexes for the first binary complex in the bacterial phosphotransferase system (the N-terminal domain of enzyme I and the phosphocarrier protein HPr). Of particular interest is the observation that the distribution of encounter complexes correlates with the electrostatic surface potentials on the interacting proteins.

Date: 2006
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DOI: 10.1038/nature05201

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