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FEBS Lett. 2009 Feb 18;583(4):815-9. doi: 10.1016/j.febslet.2009.01.035. Epub 2009 Jan 29.

Identification of the ice-binding face of a plant antifreeze protein.

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Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6.


The antifreeze protein of Lolium perenne, a perennial ryegrass, was previously modeled as a beta-roll with two extensive flat beta-sheets on opposite sides of the molecule. Here we have validated the model with a series of nine site-directed steric mutations in which outward-pointing short side-chain residues were replaced by tyrosine. None of these disrupted the fold. Mutations on one of the beta-sheets and on the sides of the protein retained 70% or greater activity. Three mutations that clustered on the other flat surface lost up to 90% of their antifreeze activity and identify this beta-sheet as the ice-binding face.

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