title: The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes.
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.
authors.affiliation: Department of Experimental Medicine, University of Parma, Via Volturno, 39, 43100 Parma, Italy.
authors.forename: Thelma A
authors.initials: TA
authors.lastname: Pertinhez
authors.forename: Elena
authors.initials: E
authors.lastname: Ferrari
authors.forename: Emanuela
authors.initials: E
authors.lastname: Casali
authors.forename: Jital A
authors.initials: JA
authors.lastname: Patel
authors.forename: Alberto
authors.initials: A
authors.lastname: Spisni
authors.forename: Lorna J
authors.initials: LJ
authors.lastname: Smith
mesh_terms: D000818:Animals; D008024:Ligands; D051379:Mice; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D008024:Ligands; D011506:Proteins; C035737:major urinary proteins