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 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.
| Original language | English |
|---|---|
| Pages (from-to) | 852-855 |
| Number of pages | 4 |
| Journal | Nature Biotechnology |
| Volume | 24 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2006 |
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ASJC Scopus subject areas
- Microbiology
Cite this
Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. / Doxey, Andrew C.; Yaish, Mahmoud W.; Griffith, Marilyn; McConkey, Brendan J.
In: Nature Biotechnology, Vol. 24, No. 7, 07.2006, p. 852-855.Research output: Contribution to journal › Article
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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.
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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UR - http://www.scopus.com/inward/citedby.url?scp=33746106845&partnerID=8YFLogxK
U2 - 10.1038/nbt1224
DO - 10.1038/nbt1224
M3 - Article
C2 - 16823370
AN - SCOPUS:33746106845
VL - 24
SP - 852
EP - 855
JO - Nature Biotechnology
JF - Nature Biotechnology
SN - 1087-0156
IS - 7
ER -