Structural basis of pheromone binding to mouse major urinary protein (MUP-I)

The mouse major urinary proteins are pheromone-binding proteins that functi on as carriers of volatile effecters of mouse physiology and behavior. Crys tal structures of recombinant mouse major urinary protein-I (MUP-I) complex ed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hyd roxy-6-methyl-3-heptanone, have been determined at high resolution. The pur ification of MUP-I from mouse liver and a high-resolution structure of the natural isolate are also reported. These results show the binding of 6-hydr oxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how differen t chemical classes of pheromones can be accommodated within the MUP-I beta -barrel.