期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 390, 期 4, 页码 1266-1271出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.10.133
关键词
Major urinary protein; Lipocalin; Ligand binding; NMR; Protein dynamics; Chemical shift
资金
- Royal Society
- Marie Curie Incoming International Fellowship [MIFI-CF-2005-022050]
- MIUR, Italy
N-15 and (HN)-H-1 chemical shift data and N-15 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. (C) 2009 Elsevier Inc. All rights reserved.
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