| Title: | The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes |
| Author(s): | Pertinhez TA; Ferrari E; Casali E; Patel JA; Spisni A; Smith LJ; |
| Address: | "Department of Experimental Medicine, University of Parma, Via Volturno, 39, 43100 Parma, Italy" |
| Journal Title: | Biochem Biophys Res Commun |
| DOI: | 10.1016/j.bbrc.2009.10.133 |
| ISSN/ISBN: | 1090-2104 (Electronic) 0006-291X (Linking) |
| 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" |
| Keywords: | "Animals Ligands Mice Protein Binding Protein Structure, Secondary Proteins/chemistry/genetics/*metabolism;" |
| Notes: | "MedlinePertinhez, Thelma A Ferrari, Elena Casali, Emanuela Patel, Jital A Spisni, Alberto Smith, Lorna J eng Research Support, Non-U.S. Gov't 2009/11/03 Biochem Biophys Res Commun. 2009 Dec 25; 390(4):1266-71. doi: 10.1016/j.bbrc.2009.10.133. Epub 2009 Oct 28" |
