Journal
NATURE CHEMISTRY
Volume 4, Issue 7, Pages 527-533Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1342
Keywords
-
Categories
Funding
- NUI Galway
- Science Foundation Ireland [07/IN.1/B975, 07/RFP/BICF236]
- Science Foundation Ireland (SFI) [07/RFP/BICF236, 07/IN.1/B975] Funding Source: Science Foundation Ireland (SFI)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available