Antifreeze protein

Insect antifreeze protein, Tenebrio-type
Structure of the Tenebrio molitor beta-helical antifreeze protein[1]
Identifiers
SymbolAFP
PfamPF02420
InterProIPR003460
SCOP21ezg / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Insect antifreeze protein (CfAFP)
Structure of Choristoneura fumiferana (spruce budworm) beta-helical antifreeze protein[2]
Identifiers
SymbolCfAFP
PfamPF05264
InterProIPR007928
SCOP21m8n / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Fish antifreeze protein, type I
Identifiers
Symbol?
InterProIPR000104
SCOP21wfb / SCOPe / SUPFAM
Fish antifreeze protein, type II
Identifiers
Symbol?
InterProIPR002353
CATH2py2
SCOP22afp / SCOPe / SUPFAM
Fish antifreeze protein, type III
Identifiers
Symbol?
InterProIPR006013
SCOP21hg7 / SCOPe / SUPFAM
See also the SAF domain (InterProIPR013974).
Ice-binding protein-like (sea ice organism)
Identifiers
SymbolDUF3494
PfamPF11999
InterProIPR021884
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Antifreeze proteins (AFPs) or ice structuring proteins refer to a class of polypeptides produced by certain animals, plants, fungi and bacteria that permit their survival in temperatures below the freezing point of water. AFPs bind to small ice crystals to inhibit the growth and recrystallization of ice that would otherwise be fatal.[3] There is also increasing evidence that AFPs interact with mammalian cell membranes to protect them from cold damage. This work suggests the involvement of AFPs in cold acclimatization.[4]

  1. ^ Daley ME, Spyracopoulos L, Jia Z, Davies PL, Sykes BD (April 2002). "Structure and dynamics of a beta-helical antifreeze protein". Biochemistry. 41 (17): 5515–25. doi:10.1021/bi0121252. PMID 11969412.
  2. ^ Leinala EK, Davies PL, Doucet D, Tyshenko MG, Walker VK, Jia Z (September 2002). "A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights". The Journal of Biological Chemistry. 277 (36): 33349–52. doi:10.1074/jbc.M205575200. PMID 12105229.
  3. ^ Goodsell D (December 2009). "Molecule of the Month: Antifreeze Proteins". The Scripps Research Institute and the RCSB PDB. doi:10.2210/rcsb_pdb/mom_2009_12. Archived from the original on 2015-11-04. Retrieved 2012-12-30.
  4. ^ Fletcher GL, Hew CL, Davies PL (2001). "Antifreeze proteins of teleost fishes". Annual Review of Physiology. 63: 359–90. doi:10.1146/annurev.physiol.63.1.359. PMID 11181960.