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

¹ Department of Biochemistry, Indiana University, Indianapolis, Indiana 46202, USA
² Institute for Pheromone Research, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA

Reprint requests to: David E. Timm, Department of Biochemistry, Indiana University, 635 Barnhill Drive, Indianapolis, Indiana 46202, USA; e-mail: dtimm{at}iupui.edu; fax: (317) 274-4686.

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 ß-barrel.

Keywords: Pheromone; crystal structure; lipocalin; binding protein; X-ray crystallography

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