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A Sensor, A Switch, A Zipper: Protein Engineers Design Potential Tool

P>Manipulation of coiled coils may also allow scientists to attach specific proteins together. In nature, coiled coils "zip" together two or more subunits of a protein. To take advantage of this functionality, scientists would fuse one protein to a coiled coil and fuse another protein to a loose helix, then add benzene to drive the formation of a triple helix. One example of such an application is to bring together a DNA-binding protein and a gene-activating protein to create a "switch" that targets and activates a specific gene.

The goal of protein engineers is to design and build proteins with desired three-dimensional shapes, which are crucial to protein function. Predicting the shape of a designed protein is a daunting task, because scientists don't fully understand how proteins fold into their final structure. To confront this difficulty, the Berkeley group started with a protein whose structure is known. Using their knowledge of protein architecture, they determined how to generate the desired structure--a triple helix. After synthesizing this newly designed protein, the scientists used x-ray crystallography to determine its three-dimensional shape. The result confirmed, with a clarity unusual in the field, that they had successfully predicted the final structure.

Beyond any potential applications, this study helps increase general understanding of coiled coils. These structures are found in hundreds of proteins and are essential to processes as diverse as gene transcription, muscle contraction, viral attack, and cell division.

Please acknowledge partial funding for this work from the National Institute of General Medical Sciences (NIGMS), a component of the Nationa
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Contact: Alisa Zapp
zappa@gm1.nigms.nih.gov
301-496-7301
NIH/National Institute of General Medical Sciences
31-Dec-1996


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