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

Pertinhez, TA; Ferrari, E; Casali, E; Patel, JA; Spisni, A; Smith, LJ

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 diff...

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APA Style

Pertinhez, T. A., Ferrari, E., Casali, E., Patel, J. A., Spisni, A., & Smith, L. J. (2009). The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. Biochemical and Biophysical Research Communications, 390(4), 1266–1271.

MLA Style

Pertinhez, T. A., et al. “The Binding Cavity of Mouse Major Urinary Protein Is Optimised for a Variety of Ligand Binding Modes.” Biochemical and Biophysical Research Communications, vol. 390, no. 4, Biochemical and biophysical research communications, 2009, pp. 1266–71.

Chicago Style

Pertinhez, TA, E Ferrari, E Casali, JA Patel, A Spisni, and LJ Smith. 2009. “The Binding Cavity of Mouse Major Urinary Protein Is Optimised for a Variety of Ligand Binding Modes.” Biochemical and Biophysical Research Communications 390 (4): 1266–71.
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