Nature Biotechnology 24, 852 - 855 (2006)
Published online: 2 July 2006; | doi:10.1038/nbt1224
Ordered surface carbons distinguish antifreeze proteins and their ice-binding regionsAndrew C Doxey1, Mahmoud W Yaish1, 2, Marilyn Griffith1
& Brendan J McConkey11
Department of Biology, University of Waterloo, 200 University Avenue West, Waterloo, Ontario
N2L 3G1, Canada. 2
Current address: Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, N1G 2W1
Canada.
Correspondence should be addressed to Brendan J McConkey mcconkey@uwaterloo.ca 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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