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Updated: Jun 19, 2026

Optimizing Mouse Urodynamic Techniques for Improved Accuracy
Published on: June 7, 2024
The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes
Thelma A Pertinhez1, Elena Ferrari, Emanuela Casali
1Department of Experimental Medicine, University of Parma, Via Volturno, 39, 43100 Parma, Italy.
Abstract:
(15)N and (1)HN chemical shift data and (15)N relaxation studies have been used to characterise the binding of N-phenyl-naphthylamine (NPN) to mouse major urinary protein (MUP). NPN binds in the beta-barrel cavity of MUP, hydrogen bonding to Tyr120 and making extensive non-bonded contacts with hydrophobic side chains. In contrast to the natural pheromone 2-sec-butyl-4,5-dihydrothiazole, NPN binding gives no change to the overall mobility of the protein backbone of MUP. Comparison with 11 different ligands that bind to MUP shows a range of binding modes involving 16 different residues in the beta-barrel cavity. These finding justify why MUP is able to adapt to allow for many successful binding partners.
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