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

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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Publication status:
Published

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Publisher copy:
10.1016/j.bbrc.2009.10.133

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Journal:
Biochemical and biophysical research communications
Volume:
390
Issue:
4
Pages:
1266-1271
Publication date:
2009-12-05
DOI:
EISSN:
1090-2104
ISSN:
0006-291X
URN:
uuid:714980a7-6792-4795-9ec1-7168d21d0b40
Source identifiers:
41487
Local pid:
pubs:41487

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