1i04
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(New page: 200px<br /><applet load="1i04" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i04, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 14:49, 20 November 2007
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CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN-I FROM MOUSE LIVER
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
1I04 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
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