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Recent Advances in Structural Studies of Antifreeze Proteins

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Title
Recent Advances in Structural Studies of Antifreeze Proteins
Other Titles
구조 생물학을 이용한 Antifreeze protein의 최근 연구동향
Authors
Lee, Sung Gu
Kim, Hak Jun
Lee, Jun Hyuck
Subject
Oceanography
Keywords
NMR; X-ray crystallography; antifreeze protein; ice binding protein; structural biology
Issue Date
2011
Publisher
Ocean and Polar Research
Citation
Lee, Sung Gu, Kim, Hak Jun, Lee, Jun Hyuck. 2011. "Recent Advances in Structural Studies of Antifreeze Proteins". Ocean and Polar Research, 33: 159-169.
Abstract
Antifreeze proteins (AFPs) have ice binding affinity, depress freezing temperature and inhibit ice recystallization which protect cellular membranes in polar organisms. Recent structural studies of antifreeze proteins have significantly expanded our understanding of the structure-function relationship and ice crystal growth inhibition. Although AFPs (Type I-IV AFP from fish, insect AFP and Plant AFP) have completely different fold and no sequence homology, they share a common feature of their surface area for ice binding property. The conserved ice-binding sites are relatively flat and hydrophobic. For example, Type I AFP has an amphipathic, single α-helix and has regularly spaced Thr-Ala residues which make direct interaction with oxygen atoms of ice crystals. Unlike Type I AFP, Type II and III AFP are compact globular proteins that contain a flat ice-binding patch on the surface. Type II and Type III AFP show a remarkable structural similarity with the sugar binding lectin protein and C-terminal domain of sialic acid synthase, respectively. Type IV is assumed to form a four-helix bundle which has sequence similarity with apolipoprotein. The results of our modeling suggest an ice-binding induced structural change of Type IV AFP. Insect AFP has β-helical structure with a regular array of Thr-X-Thr motif. Threonine residues of each Thr-X-Thr motif fit well into the ice crystal lattice expanded our understanding of the structure-function relationship and ice crystal growth inhibition. Although AFPs (Type I-IV AFP from fish, insect AFP and Plant AFP) have completely different fold and no sequence homology, they share a common feature of their surface area for ice binding property. The conserved ice-binding sites are relatively flat and hydrophobic. For example, Type I AFP has an amphipathic, single α-helix and has regularly spaced Thr-Ala residues which make direct interaction with oxygen atoms of ice crystals. Unlike Type
URI
http://repository.kopri.re.kr/handle/201206/6534
DOI
http://dx.doi.org/10.4217/OPR.2011.33.2.159
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