Publication Abstract from PubMed
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.
Structural basis of pheromone binding to mouse major urinary protein (MUP-I).,Timm DE, Baker LJ, Mueller H, Zidek L, Novotny MV Protein Sci. 2001 May;10(5):997-1004. PMID:11316880[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
