| First Author | Timm DE | Year | 2001 |
| Journal | Protein Sci | Volume | 10 |
| Issue | 5 | Pages | 997-1004 |
| PubMed ID | 11316880 | Mgi Jnum | J:172899 |
| Mgi Id | MGI:5009190 | Doi | 10.1110/ps.52201 |
| Citation | Timm DE, et al. (2001) Structural basis of pheromone binding to mouse major urinary protein (MUP-I). Protein Sci 10(5):997-1004 |
| abstractText | The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effectors 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. |
