1i05

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Revision as of 14:49, 20 November 2007

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spinqualitylabelsall models 1i05, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with CD and LTL as ligands. 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

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