Abstract: 15N and 1HN chemical shift data and 15N relaxation studies have been used to characterise the binding of N-phenyl-naphthylamine (NPN) to mouse major urinary protein (MUP). NPN binds in the b-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 b-barrel cavity. These finding justify why MUP is able to adapt to allow for many successful binding partners.

The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes / Pertinhez, Thelma; Ferrari, Elena; Casali, Emanuela; J. A., Patel; Spisni, Alberto; L. J., Smith. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 390:(2009), pp. 1266-1271. [10.1016/j.bbrc.2009.10.133]

The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes

PERTINHEZ, Thelma;FERRARI, Elena;CASALI, Emanuela;SPISNI, Alberto;
2009-01-01

Abstract

Abstract: 15N and 1HN chemical shift data and 15N relaxation studies have been used to characterise the binding of N-phenyl-naphthylamine (NPN) to mouse major urinary protein (MUP). NPN binds in the b-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 b-barrel cavity. These finding justify why MUP is able to adapt to allow for many successful binding partners.
The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes / Pertinhez, Thelma; Ferrari, Elena; Casali, Emanuela; J. A., Patel; Spisni, Alberto; L. J., Smith. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 390:(2009), pp. 1266-1271. [10.1016/j.bbrc.2009.10.133]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/2303434
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