Alt a 1 defines a new homologous protein family with unknown function exclusively found in fungi. The unique structure of Alt a 1 contains intramolecular disulfide bonds that are conserved among the Alt a 1 homologs. Residues reported to be IgE antibody-binding epitopes are exposed through dimerization via a conserved disulfide bond and hydrophobic and polar interactions. Further mechanistic structure/function studies will give insight into immunologic studies directed toward new forms of immunotherapy for Alternaria species-sensitive allergic patients.
Comment:Although Alt a 1 normally forms a dimer, it runs as a pair of monomers in reducing SDS-PAGE, consistent with a disulfide linkage between the monomers
Jiyao W et al.(2023). "The conserved domain database in 2023.",