Designing proteins with cavities

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Science  13 Jan 2017:
Vol. 355, Issue 6321, pp. 143
DOI: 10.1126/science.355.6321.143-b

In de novo protein design, creating custom-tailored binding sites is a particular challenge because these sites often involve nonideal backbone structures. For example, curved b sheets are a common ligand binding motif. Marcos et al. investigated the principles that drive β-sheet curvature by studying the geometry of β sheets in natural proteins and folding simulations. In a step toward custom design of enzyme catalysts, they used these principles to control β-sheet geometry and design proteins with differently shaped cavities.

Science, this issue p. 201

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