Structural basis of pheromone binding to mouse major urinary protein (MUP-I).
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.
Timm
D E
DE
Department of Biochemistry, Indiana University, Indianapolis, Indiana 46202, USA. dtimm@iupui.edu
Baker
L J
LJ
Mueller
H
H
Zidek
L
L
Novotny
M V
MV
D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008099:Liver / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D010675:Pheromones / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010675:Pheromones; D011506:Proteins; C035737:major urinary proteins