Pheromone specificity in the Lepidoptera is encoded in protein components of the antennal sensillum lymph and dendritic membrane. In this paper, we highlight recent work on the molecular determinants of pheromone binding affinity of pheromone binding proteins (PBPs) of three genera. First, we describe new cDNA sequences for Lymantria dispar (Lymantriidae) and Agrotis segetum (Noctuidae). These data enrich the conclusions derived from our functional studies. Secondly, we indicate how preparation of multimilligram quantities of the recombinant PBP 'Apol-3' (originally from Antheraea polyphemus) has provided a platform (i) to determine the ligand binding sites using photoaffinity labeling, (ii) to conduct structural analysis by CD and NMR, and (iii) to measure binding affinities using a new binding assay. Thirdly, we describe the use of expression-cassette PCR technology to prepare two related PBPs from Antheraea perneyi to test binding affinities of naturally-occurring homologous PBPs. Our results support a model in which ligand specificity for chain length, double bond position, and terminal functionality is partially encoded in the PBPs. We propose that the final decoding is accomplished when the PBP-pheromone complex activates a G-protein coupled seven-transmembrane domain receptor that contains recognition sites for both the presented pheromone and the presenting PBP.