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Solution structure of a recombinant mouse major urinary protein
C Lücke1, L Franzoni, F Abbate
1Institute of Biophysical Chemistry, J.W. Goethe-University of Frankfurt, Germany.
European Journal of Biochemistry
|December 3, 1999
Summary
Major urinary proteins (MUPs) are pheromones in mice. This study reveals the refined 3D solution structure of rMUP, showing its beta-barrel structure is key for binding hydrophobic odorants.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Major urinary proteins (MUPs) are pheromones in male mice, belonging to the lipocalin superfamily.
- MUPs bind hydrophobic odorants and interact with female vomeronasal organs, influencing reproductive cycles.
- The exact structural and dynamical features of MUPs in solution are not fully understood.
Purpose of the Study:
- To determine the high-resolution three-dimensional solution structure of a specific rMUP isoform.
- To investigate the structural basis for MUPs' ligand-binding capabilities.
- To compare the solution structure with known crystal structures.
Main Methods:
- Cloning and isotopic labeling of the rMUP isoform.
- Multidimensional heteronuclear Nuclear Magnetic Resonance (NMR) experiments for resonance assignment.
- Distance geometry and energy minimization calculations using NOE-derived distance restraints.
Main Results:
- A refined 3D solution structure of rMUP was obtained.
- The structure features eight antiparallel beta-strands forming a beta-sheet and a C-terminal alpha-helix.
- The tertiary fold creates a calyx-shaped beta-barrel lined with hydrophobic residues, consistent with ligand binding.
Conclusions:
- The solution structure of rMUP closely resembles its crystal structure, with minor differences.
- The conserved beta-barrel structure is crucial for binding and transporting hydrophobic molecules.
- This structural insight aids in understanding MUPs' function as pheromones.