Linked Life Data

19878650

Source:http://linkedlifedata.com/resource/pubmed/id/19878650

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SubjectPredicateObjectContext
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pubmed-article:19878650pubmed:abstractText(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.lld:pubmed
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pubmed-article:19878650pubmed:authorpubmed-author:SmithLorna...lld:pubmed
pubmed-article:19878650pubmed:authorpubmed-author:PertinhezThel...lld:pubmed
pubmed-article:19878650pubmed:authorpubmed-author:SpisniAlberto...lld:pubmed
pubmed-article:19878650pubmed:authorpubmed-author:FerrariElenaElld:pubmed
pubmed-article:19878650pubmed:authorpubmed-author:CasaliEmanuel...lld:pubmed
pubmed-article:19878650pubmed:authorpubmed-author:PatelJital...lld:pubmed
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pubmed-article:19878650pubmed:day25lld:pubmed
pubmed-article:19878650pubmed:volume390lld:pubmed
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pubmed-article:19878650pubmed:pagination1266-71lld:pubmed
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pubmed-article:19878650pubmed:year2009lld:pubmed
pubmed-article:19878650pubmed:articleTitleThe binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes.lld:pubmed
pubmed-article:19878650pubmed:affiliationDepartment of Experimental Medicine, University of Parma, Via Volturno, 39, 43100 Parma, Italy.lld:pubmed
pubmed-article:19878650pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19878650pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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