Abstract
Antifreeze proteins (AFPs) are found in cold-adapted organisms and have the unusual ability to bind to and inhibit the growth of ice crystals. However, the underlying molecular basis of their ice-binding activity is unclear because of the difficulty of studying the AFP-ice interaction directly and the lack of a common motif, domain or fold among different AFPs. We have formulated a generic ice-binding model and incorporated it into a physicochemical pattern-recognition algorithm. It successfully recognizes ice-binding surfaces for a diverse range of AFPs, and clearly discriminates AFPs from other structures in the Protein Data Bank1. The algorithm was used to identify a novel AFP from winter rye, and the antifreeze activity of this protein was subsequently confirmed. The presence of a common and distinct physicochemical pattern provides a structural basis for unifying AFPs from fish, insects and plants.
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Acknowledgements
We would like to dedicate this publication to the memory of Marilyn Griffith. This work was supported by grants from the National Science and Engineering Research Council (NSERC) to B.J.M. and M.G., and we acknowledge the Killam Research Fellowship Program on behalf of M.G. We thank Barbara Moffatt for providing T. salsuginea sequences and Bernard Duncker for comments on the manuscript.
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Supplementary information
Supplementary Fig. 1
Ordered surface carbons detected in known AFPs. (PDF 1064 kb)
Supplementary Fig. 2
Correlation between type III mutant thermal hysteresis values and algorithm score. (PDF 64 kb)
Supplementary Fig. 3
Algorithm for prediction of ordered surface carbons. (PDF 68 kb)
Supplementary Table 1
Residues contributing predicted ordered surface carbons. (PDF 47 kb)
Supplementary Table 2
Comparison of algorithm performance with individual components omitted. (PDF 37 kb)
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Doxey, A., Yaish, M., Griffith, M. et al. Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. Nat Biotechnol 24, 852–855 (2006). https://doi.org/10.1038/nbt1224
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DOI: https://doi.org/10.1038/nbt1224
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