Publication details

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

Authors

TIMM David E. BAKER L. J. MUELLER H ŽÍDEK Lukáš NOVOTNY Milos

Year of publication 2001
Type Article in Periodical
Magazine / Source Protein Science
MU Faculty or unit

Faculty of Science

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.

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