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