Peer-Reviewed Journal Details
Mandatory Fields
McGovern, RE,Fernandes, H,Khan, AR,Power, NP,Crowley, PB
2012
July
Nature Chemistry
Protein camouflage in cytochrome c-calixarene complexes
Published
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Optional Fields
SURFACE RECOGNITION NMR-SPECTROSCOPY AMINO-ACIDS CRYSTALLIZATION STRATEGY LYSINE MOLECULES STATE CRYSTALLOGRAPHY VALIDATION
4
527
533
Small molecules that recognize protein surfaces are important tools for modifying protein interaction properties. Since the 1980s, several thousand studies concerning calixarenes and host-guest interactions have been published. Although there is growing interest in protein-calixarene interactions, only limited structural information has been available to date. We now report the crystal structure of a protein-calixarene complex. The water-soluble p-sulfonatocalix[4]arene is shown to bind the lysine-rich cytochrome c at three different sites. Binding curves obtained from NMR titrations reveal an interaction process that involves two or more binding sites. Together, the data indicate a dynamic complex in which the calixarene explores the surface of cytochrome c. In addition to providing valuable information on protein recognition, the data also indicate that the calixarene is a mediator of protein-protein interactions, with potential applications in generating assemblies and promoting crystallization.
DOI 10.1038/NCHEM.1342
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