Publication details
Structural basis of pheromone binding to mouse major urinary protein (MUP-I)
| Authors | |
|---|---|
| Year of publication | 2001 |
| Type | Article in Periodical |
| Magazine / Source | Protein Science |
| MU Faculty or unit | |
| Citation | |
| Keywords | FEMALE MICE; HOUSE MOUSE; PUBERTY; RESOLUTION; CRYSTALLOGRAPHY; REFINEMENT; LIPOCALIN; MUSCULUS; LIGAND; GENES |
| Description | The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effecters of mouse physiology and behavior. Crystal structures of recombinant mouse major urinary protein-I (MUP-I) complexed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hydroxy-6-methyl-3-heptanone, have been determined at high resolution. The purification 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-hydroxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how different chemical classes of pheromones can be accommodated within the MUP-I beta -barrel. |