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

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.

SUBMITTER: Timm DE

PROVIDER: S-EPMC2374202 | biostudies-literature | 2001 May

REPOSITORIES: biostudies-literature

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

Timm D E DE Baker L J LJ Mueller H H Zidek L L Novotny M V MV

Protein science : a publication of the Protein Society 20010501 5

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 s ...[more]

PMID: 11316880

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