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|1io6, 1 NMR models ()|
GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 (GRB2) C-TERMINAL SH3 DOMAIN COMPLEXED WITH A LIGAND PEPTIDE (NMR, MINIMIZED MEAN STRUCTURE)
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.
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:011316880
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Timm DE, Baker LJ, Mueller H, Zidek L, Novotny MV. Structural basis of pheromone binding to mouse major urinary protein (MUP-I). Protein Sci. 2001 May;10(5):997-1004. PMID:11316880