Solution structure of a recombinant mouse major urinary protein.

By C. Lücke, L. Franzoni, F. Abbate, F. Löhr, E. Ferrari, R. Sorbi, H. Rüterjans, A. Spisni. 1999

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Polymorphism in Major Urinary Proteins: Molecular Heterogeneity in a Wild Mouse Population (2002, background): “These MUPs are lipocalins (Flower et al., 1993), characterized by an archetypical eight-stranded β-barrel (Bocskei et al., 1992; Lucke et al., 1999; Zidek et al., 1999), enclosing a hydrophobic cavity.”
The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. (2009, methodology): “N labelled recombinant wild-type MUP and a Y120F mutant were expressed in Pichia pastoris in minimum media and purified as described previously [6,7].”
Molecular dynamics study of major urinary protein–pheromone interactions: A structural model for ligand‐induced flexibility increase (2006, methodology): “To obtain dynamic information corresponding to the results of 15N NMR relaxation measurements, correlation functions for intramolecular motion, and subsequently the order parameter S2 of NH bond vectors, were calculated using a standard procedure [8].”
Pheromone binding by polymorphic mouse major urinary proteins (2002, methodology): “In addition, we have characterized the interactions between SBT and MUP-I in solution using NMR spectroscopy (Zidek et al. 1999), and an NMR structure of recombinant MUP-II has also been reported (Lucke et al. 1999).”