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

Protein Sci. 2001 May;10(5):997-1004. doi: 10.1110/ps.52201.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Liver / chemistry
  • Mice
  • Models, Molecular
  • Pheromones / chemical synthesis
  • Pheromones / chemistry
  • Pheromones / metabolism*
  • Protein Binding
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Structure-Activity Relationship


  • Pheromones
  • Proteins
  • major urinary proteins

Associated data

  • PDB/1IO4
  • PDB/1IO5
  • PDB/1IO6