According to the structure and function study on the antifreeze protein from Pseudopleuronectes americanus, the antifreeze mechanism of the type-I AFP molecule was shown to be due to the binding to an ice nucleation structure in a zipper-like fashion through hydrogen bonding of the hydroxyl groups of its four Thr residues to the oxygens along the  direction in ice lattice, subsequently stopping or retarding the growth of ice pyramidal planes so as to depress the freeze point.
The above mechanism can be used to elucidate the structure-function relationship of other antifreeze proteins with the following two common features:
# recurrence of a Thr residue (or any other polar amino acid residue whose side-chain can form a hydrogen bond with water) in an 11-amino-acid period along the sequence concerned, and
# a high percentage of an Ala residue component therein.