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Four of the strands dominate the global fold, and 2 of the helices form a C-terminal amphipathic helical motif. This motif is believed to be the T-cell epitope.
However, one very striking feature of the three-dimensional structure of Bet v 1 is the presence of a large hydrophobic cavity, which is open to the exterior and probably functions as a ligand binding site.
The biological function of Bet v 1 is still under investigations. Bet v 1 harbors a large hydrophobic pocket and is able to bind a large spectra of ligands in it like hormones  and siderophores like flavenols.
It belongs to the pathogenesis-related PR proteins, which are usually expressed upon infections and stressful conditions,  implicating a role in host defense.
In vitro , Bet v 1 has been shown to be immune-suppressive, when its pocket was filled by a ligand, but was able to mount a Th2-response important in allergy development, when the pocket remained empty.