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  • Title: The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes.
    Author: Pertinhez TA, Ferrari E, Casali E, Patel JA, Spisni A, Smith LJ.
    Journal: Biochem Biophys Res Commun; 2009 Dec 25; 390(4):1266-71. PubMed ID: 19878650.
    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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