Antifreeze proteins: an unusual receptor-ligand interaction.
Antifreeze proteins (AFPs) help organisms to survive below 0 degrees C by inhibiting ice growth. Although AFPs are structurally diverse, they typically present a large proportion of their surface area for binding to ice. Whereas earlier proposed binding mechanisms relied almost entirely on a hydrogen bond match between the AFP and ice, it now seems probable that van der Waals and hydrophobic interactions make a significant contribution to the enthalpy of adsorption. These interactions require intimate surface-surface complementarity between the receptor (AFP) and its ligand (ice).
Jia
Zongchao
Z
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6.
Davies
Peter L
PL
D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D005399:Fishes / Q000502:physiology; D007313:Insecta / Q000502:physiology; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D021301:Antifreeze Proteins; D008024:Ligands