Protein Domain : Haemolymph juvenile hormone binding IPR010562

Type  Family
Description  This family consists of several insect specific haemolymph juvenile hormone binding proteins (JHBP). Juvenile hormone (JH) has a profound effect on insects. It regulates embryogenesis, maintains the status quo of larva development and stimulates reproductive maturation in the adult forms. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph [ ]. The crystal structure of the JHBP from Galleria mellonella (Wax moth) shows an unusual fold consisting of a long α-helix wrapped in a much curved antiparallel β-sheet, the so-called TULIP domain []. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organisation of the major cavity and a disulphide bond linking the long helix and the β-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance [, ].Proteins in this entry includes protein Daywake (dyw) and Takeout (to) from fruit flies [ ]. Dyw functions in neurons as a day-specific anti-siesta gene, with little effect on sleep levels during the nighttime or in the absence of light []. Protein Takeout is implicated in circadian control of feeding behaviour [, ] and affects male courtship behaviour [].
Short Name  Haemolymph_juvenile_hormone-bd

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