1i05
From Proteopedia
CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN (MUP-I) COMPLEXED WITH HYDROXY-METHYL-HEPTANONE
Overview
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.
About this Structure
1I05 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of pheromone binding to mouse major urinary protein (MUP-I)., Timm DE, Baker LJ, Mueller H, Zidek L, Novotny MV, Protein Sci. 2001 May;10(5):997-1004. PMID:11316880 Page seeded by OCA on Fri May 2 19:25:08 2008
