1I04

CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN-I FROM MOUSE LIVER

Summary for 1I04

• Entry DOI: 10.2210/pdb1i04/pdb
• Related: 1I05 1I06 1MUP
• Descriptor: MAJOR URINARY PROTEIN I (2 entities in total)
• Functional Keywords: lipocalin, beta-barrel, pheromone, transport protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 20674.40

Authors

Timm, D.E.,Baker, L.J.,Mueller, H.,Zidek, L.,Novotny, M.V. (deposition date: 2001-01-28, release date: 2001-02-14, Last modification date: 2024-10-30)

Primary citation

Timm, D.E.,Baker, L.J.,Mueller, H.,Zidek, L.,Novotny, M.V.
Structural basis of pheromone binding to mouse major urinary protein (MUP-I)
Protein Sci., 10:997-1004, 2001

PubMed Abstract: 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.

PubMed: 11316880
DOI: 10.1110/ps.52201

Experimental method

X-RAY DIFFRACTION (2 Å)