1i05
From Proteopedia
CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN (MUP-I) COMPLEXED WITH HYDROXY-METHYL-HEPTANONE
Structural highlights
FunctionMUP6_MOUSE Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
|
| |||||||||||||||||||
Categories: Large Structures | Mus musculus | Baker LJ | Mueller H | Novotny MV | Timm DE | Zidek L
