1l1i

Structural highlights

Function

ANPY1_TENMO Contributes to protect body fluid from freezing at subzero temperatures. Lowers the freezing point of the hemolymph by about 2.5 degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals and prevents further growth.^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Antifreeze protein 3D structures

References

1. ↑ Liou YC, Thibault P, Walker VK, Davies PL, Graham LA. A complex family of highly heterogeneous and internally repetitive hyperactive antifreeze proteins from the beetle Tenebrio molitor. Biochemistry. 1999 Aug 31;38(35):11415-24. PMID:10471292 doi:http://dx.doi.org/10.1021/bi990613s
2. ↑ Liou YC, Daley ME, Graham LA, Kay CM, Walker VK, Sykes BD, Davies PL. Folding and structural characterization of highly disulfide-bonded beetle antifreeze protein produced in bacteria. Protein Expr Purif. 2000 Jun;19(1):148-57. PMID:10833402 doi:http://dx.doi.org/10.1006/prep.2000.1219
3. ↑ Graham LA, Liou YC, Walker VK, Davies PL. Hyperactive antifreeze protein from beetles. Nature. 1997 Aug 21;388(6644):727-8. PMID:9285581 doi:http://dx.doi.org/10.1038/41908