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000049418 0247_ $$2DOI$$a10.1110/ps.051563605
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000049418 084__ $$2WoS$$aBiochemistry & Molecular Biology
000049418 1001_ $$0P:(DE-HGF)0$$aBauer, F.$$b0
000049418 245__ $$aStructural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity
000049418 260__ $$aHoboken, NJ$$bWiley$$c2005
000049418 300__ $$a2487 -2498
000049418 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000049418 440_0 $$010881$$aProtein Science$$v14$$x0961-8368$$y10
000049418 500__ $$aRecord converted from VDB: 12.11.2012
000049418 520__ $$aThe Src homology 3 (SH3) domain of the Src family kinase Lyn binds to the herpesviral tyrosine kinase interacting protein (Tip) more than one order of magnitude stronger than other closely related members of the Src family. In order to identify the molecular basis for high-affinity binding, the structure of free and Tip-bound Lyn-SH3 was determined by NMR spectroscopy. Tip forms additional contacts outside its classical proline-rich recognition motif and, in particular, a strictly conserved leucine (L186) of the C-terminally adjacent sequence stretch packs into a hydrophobic pocket on the Lyn surface. Although the existence of this pocket is no unique property of Lyn-SH3, Lyn is the only Src family kinase that contains an additional aromatic residue (H41) in the n-Src loop as part of this pocket. H41 covers L186 of Tip by forming tight hydrophobic contacts, and model calculations suggest that the increase in binding affinity compared with other SH3 domains can mainly be attributed to these additional interactions. These findings indicate that this pocket can mediate specificity even between otherwise closely related SH3 domains.
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000049418 588__ $$aDataset connected to Web of Science, Pubmed
000049418 650_2 $$2MeSH$$aModels, Molecular
000049418 650_2 $$2MeSH$$aMultiprotein Complexes: chemistry
000049418 650_2 $$2MeSH$$aMultiprotein Complexes: metabolism
000049418 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular: methods
000049418 650_2 $$2MeSH$$aPhosphoproteins: chemistry
000049418 650_2 $$2MeSH$$aPhosphoproteins: metabolism
000049418 650_2 $$2MeSH$$aProtein Binding
000049418 650_2 $$2MeSH$$aProtein Structure, Quaternary
000049418 650_2 $$2MeSH$$aViral Proteins: chemistry
000049418 650_2 $$2MeSH$$aViral Proteins: metabolism
000049418 650_2 $$2MeSH$$asrc Homology Domains
000049418 650_2 $$2MeSH$$asrc-Family Kinases: chemistry
000049418 650_2 $$2MeSH$$asrc-Family Kinases: metabolism
000049418 650_7 $$00$$2NLM Chemicals$$aMultiprotein Complexes
000049418 650_7 $$00$$2NLM Chemicals$$aPhosphoproteins
000049418 650_7 $$00$$2NLM Chemicals$$aViral Proteins
000049418 650_7 $$00$$2NLM Chemicals$$atyrosine kinase interacting protein, Saimiriine herpesvirus 2
000049418 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$alyn protein-tyrosine kinase
000049418 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$asrc-Family Kinases
000049418 650_7 $$2WoSType$$aJ
000049418 65320 $$2Author$$aSH3 domain
000049418 65320 $$2Author$$aLyn
000049418 65320 $$2Author$$aextended binding motif
000049418 65320 $$2Author$$aligand affinity
000049418 65320 $$2Author$$aNMR
000049418 65320 $$2Author$$astructure
000049418 65320 $$2Author$$acomplex
000049418 65320 $$2Author$$aNMR spectroscopy
000049418 65320 $$2Author$$afluorescence
000049418 65320 $$2Author$$adocking proteins
000049418 7001_ $$0P:(DE-HGF)0$$aSchweimer, K.$$b1
000049418 7001_ $$0P:(DE-HGF)0$$aMeiselbach, H.$$b2
000049418 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b3$$uFZJ
000049418 7001_ $$0P:(DE-HGF)0$$aRosch, P.$$b4
000049418 7001_ $$0P:(DE-HGF)0$$aSticht, H.$$b5
000049418 773__ $$0PERI:(DE-600)2000025-X$$a10.1110/ps.051563605$$gVol. 14, p. 2487 -2498$$p2487 -2498$$q14<2487 -2498$$tProtein science$$v14$$x0961-8368$$y2005
000049418 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253286
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000049418 9141_ $$y2005
000049418 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
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000049418 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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