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000049405 0247_ $$2DOI$$a10.1021/bi051403k
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000049405 084__ $$2WoS$$aBiochemistry & Molecular Biology
000049405 1001_ $$0P:(DE-Juel1)162212$$aTran, T.$$b0$$uFZJ
000049405 245__ $$aInsights into Human Lck SH3 Domain Binding Specificity: Different Binding Modes of Artificial and Native Ligands
000049405 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2005
000049405 300__ $$a15042 - 15052
000049405 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000049405 440_0 $$0798$$aBiochemistry$$v44$$x0006-2960$$y45
000049405 500__ $$aRecord converted from VDB: 12.11.2012
000049405 520__ $$aWe analyzed the ligand binding specificity of the lymphocyte specific kinase (Lck) SH3 domain. We identified artificial Lck SH3 ligands using phage display. In addition, we analyzed Lck SH3 binding sites within known natural Lck SH3 binding proteins using an Lck specific binding assay on membrane-immobilized synthetic peptides. On one hand, from the phage-selected peptides, representing mostly special class I' ligands, a well-defined consensus sequence was obtained. Interestingly, a histidine outside the central polyproline motif contributes significantly to Lck SH3 binding affinity and specificity. On the other hand, we confirmed previously mapped Lck SH3 binding sites in ADAM15, HS1, SLP76, and NS5A, and identified putative Lck SH3 binding sites of Sam68, FasL, c-Cbl, and Cbl-b. Without exception, the comparatively diverse Lck SH3 binding sites of all analyzed natural Lck SH3 binding proteins emerged as class II proteins. Possible explanations for the observed variations between artificial and native ligands-which are not due to significant K(D) value differences as shown by calculating Lck SH3 affinities of artificial peptide PD1-Y(-3)R as well as for peptides comprising putative Lck SH3 binding sites of NS5A, Sos, and Sam68-are discussed. Our data suggest that phage display, a popular tool for determining SH3 binding specificity, must-at least in the case of Lck-not irrevocably mirror physiologically relevant protein-ligand interactions.
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000049405 650_2 $$2MeSH$$aAmino Acid Sequence
000049405 650_2 $$2MeSH$$aBinding Sites
000049405 650_2 $$2MeSH$$aConsensus Sequence
000049405 650_2 $$2MeSH$$aHistidine: chemistry
000049405 650_2 $$2MeSH$$aHumans
000049405 650_2 $$2MeSH$$aLigands
000049405 650_2 $$2MeSH$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck): chemistry
000049405 650_2 $$2MeSH$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck): metabolism
000049405 650_2 $$2MeSH$$aPeptide Library
000049405 650_2 $$2MeSH$$aPeptides: chemistry
000049405 650_2 $$2MeSH$$aProtein Binding
000049405 650_2 $$2MeSH$$aSequence Alignment
000049405 650_2 $$2MeSH$$aTyrosine: chemistry
000049405 650_2 $$2MeSH$$asrc Homology Domains
000049405 650_7 $$00$$2NLM Chemicals$$aLigands
000049405 650_7 $$00$$2NLM Chemicals$$aPeptide Library
000049405 650_7 $$00$$2NLM Chemicals$$aPeptides
000049405 650_7 $$055520-40-6$$2NLM Chemicals$$aTyrosine
000049405 650_7 $$071-00-1$$2NLM Chemicals$$aHistidine
000049405 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck)
000049405 650_7 $$2WoSType$$aJ
000049405 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b1$$uFZJ
000049405 7001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b2$$uFZJ
000049405 7001_ $$0P:(DE-Juel1)VDB20019$$aJonas, E.$$b3$$uFZJ
000049405 7001_ $$0P:(DE-HGF)0$$aLuge, C.$$b4
000049405 7001_ $$0P:(DE-Juel1)VDB58377$$aAladag, A.$$b5$$uFZJ
000049405 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b6$$uFZJ
000049405 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi051403k$$gVol. 44, p. 15042 - 15052$$p15042 - 15052$$q44<15042 - 15052$$tBiochemistry$$v44$$x0006-2960$$y2005
000049405 8567_ $$uhttp://hdl.handle.net/2128/710$$uhttp://dx.doi.org/10.1021/bi051403k
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000049405 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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