TY - JOUR
T1 - Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions
AU - Doxey, Andrew C.
AU - Yaish, Mahmoud W.
AU - Griffith, Marilyn
AU - McConkey, Brendan J.
N1 - Funding Information:
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.
PY - 2006/7
Y1 - 2006/7
N2 - 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 Bank. 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.
AB - 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 Bank. 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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U2 - 10.1038/nbt1224
DO - 10.1038/nbt1224
M3 - Article
C2 - 16823370
AN - SCOPUS:33746106845
SN - 1087-0156
VL - 24
SP - 852
EP - 855
JO - Nature Biotechnology
JF - Nature Biotechnology
IS - 7
ER -