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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Pertinhez TA,Ferrari E,Casali E,Patel JA,Spisni A,Smith LJdoi
10.1016/j.bbrc.2009.10.133subject
Has Abstractpub_date
2009-12-25 00:00:00pages
1266-71issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(09)02124-Xjournal_volume
390pub_type
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